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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Glutamine (HMDB00641)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-06-23 16:21:16
Accession Number HMDB00641
Secondary Accession Numbers Not Available
Common Name L-Glutamine
Description Glutamine (Gln) is one of the 20 amino acids encoded by the standard genetic code. Its side chain is an amide; it is formed by replacing a side-chain hydroxyl of glutamic acid with an amine functional group. glutamine is found in foods high in proteins, such as fish, red meat, beans, and dairy products. glutamine is a supplement that is used in weightlifting, bodybuilding, endurance and other sports, as well as by those who suffer from muscular cramps or pain particularly elderly people. The main use of glutamine within the diet of either group is as a means of replenishing the body's stores of amino acids that have been used during exercise or everyday activities. Studies which are looking into problems with excessive consumption of glutamine thus far have proved inconclusive. However, normal supplementation is healthy mainly because glutamine is supposed to be supplemented after prolonged periods of exercise (for example, a workout or exercise in which amino acids are required for use) and replenishes amino acid stores; this being the main reason glutamine is recommended during fasting or for people who suffer from physical trauma, immune deficiencies, or cancer. There is a significant body of evidence that links glutamine-enriched diets with intestinal effects; aiding maintenance of gut barrier function, intestinal cell proliferation and differentiation, as well as generally reducing septic morbidity and the symptoms of Irritable Bowel Syndrome. The reason for such "cleansing" properties is thought to stem from the fact that the intestinal extraction rate of glutamine is higher than that for other amino acids, and is therefore thought to be the most viable option when attempting to alleviate conditions relating to the gastrointestinal tract. These conditions were discovered after comparing plasma concentration within the gut between glutamine-enriched and non glutamine-enriched diets. However, even though glutamine is thought to have "cleansing" properties and effects, it is unknown to what extent glutamine has clinical benefits, due to the varied concentrations of glutamine in varieties of food. It is also known that glutamine has various effects in reducing healing time after operations. Hospital waiting times after abdominal surgery are reduced by providing parenteral nutrition regimens containing amounts of glutamine to patients. Clinical trials have revealed that patients on supplementation regimes containing glutamine have improved nitrogen balances, generation of cysteinyl-leukotrienes from polymorphonuclear neutrophil granulocytes and improved lymphocyte recovery and intestinal permeability (in postoperative patients) - in comparison to those who had no glutamine within their dietary regime; all without any side-effects. (http://en.wikipedia.org/wiki/glutamine)
Synonyms
  1. (2S)-2,5-diamino-5-oxopentanoic acid
  2. (2S)-2-amino-4-carbamoylbutanoic acid
  3. (S)-2,5-Diamino-5-oxopentanoic acid
  4. 2-Aminoglutaramic acid
  5. Cebrogen
  6. Glavamin
  7. Glumin
  8. Glutamic acid 5-amide
  9. Glutamic acid amide
  10. Glutamine
  11. L-(+)-glutamine
  12. L-2-Aminoglutaramic acid
  13. L-2-Aminoglutaramidic acid
  14. L-Glutamic acid 5-amide
  15. L-Glutaminsaeure-5-amid
  16. L-glutamic acid gamma-amide
  17. L-glutamid
  18. L-glutamide
  19. L-glutamin
  20. L-glutamine
  21. Levoglutamid
  22. Levoglutamida
  23. Levoglutamide
  24. Levoglutamidum
  25. Levoglutamina
  26. Polyglutamine
  27. Stimulina
  28. gamma-glutamine
  29. (2S)-2,5-diamino-5-oxopentanoate
  30. (2S)-2-amino-4-carbamoylbutanoate
  31. (S)-2,5-Diamino-5-oxopentanoate
Chemical IUPAC Name (2S)-2-amino-4-carbamoyl-butanoic acid
Chemical Formula C5H10N2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • primary carboxylic acid amide
  • alpha-aminoacid
Biofunction
  • Essential amino acid
  • Energy source
  • Non-essential amino acid
  • RNA component
  • Component of Alanine and aspartate metabolism
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Aminosugars metabolism
  • Component of D-Glutamine and D-glutamate metabolism
  • Component of Glutamate metabolism
  • Component of Nitrogen metabolism
  • Component of Peptidoglycan biosynthesis
  • Component of Purine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 146.145
Monoisotopic Molecular Weight 146.069138
Isomeric SMILES N[C@@H](CCC(N)=O)C(O)=O
Canonical SMILES NC(CCC(N)=O)C(O)=O
KEGG Compound ID C00064 Link Image
BioCyc ID GLN Link Image
BiGG ID 33714 Link Image
Wikipedia Link L-Glutamine Link Image
NuGOwiki Link HMDB00641 Link Image
Metagene Link HMDB00641 Link Image
METLIN ID 5614 Link Image
PubChem Compound 5961 Link Image
PubChem Substance 10527678 Link Image
ChEBI ID 18050 Link Image
CAS Registry Number 56-85-9
InChI Identifier InChI=1/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1
Synthesis Reference Jiao, Qingcai; Qian, Shaosong; Chen, Ran; Wu, Xiaoyan. Synthesis of L-glutamine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 7 pp.
Melting Point (Experimental) 185 oC
Experimental Water Solubility 41.3 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 41.3 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 97.799995 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.64 [CHMELIK,J ET AL. (1991)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.32 [Predicted by ALOGPS]; -4.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1CT9 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue —
Fibroblasts —
Gut —
Intestine —
Kidney —
Muscle —
Myelin —
Neuron —
Pancreas —
Placenta —
Skeletal Muscle —
Spleen —
Stratum Corneum —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 586.0 (502.0-670.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 591.0 +/- 66.0 uM
Age Children:1-13 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 645.0 +/- 64.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 578.0 +/- 85.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 905.0 +/- 250.0 uM
Age Newborn:0-30 days old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 600.0 +/- 70.0 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 490.6 +/- 84.3 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Grant SL, Shulman Y, Tibbo P, Hampson DR, Baker GB: Determination of d-serine and related neuroactive amino acids in human plasma by high-performance liquid chromatography with fluorimetric detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Dec 5;844(2):278-82. Epub 2006 Aug 4. [PubMed Link Image]
Biofluid Blood
Value 542.5 (376.0-709.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid CSF
Value 444.0 +/- 84.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 627.0 (482.0-772.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
Biofluid CSF
Value 570.0 +/- 240.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Commodari F, Arnold DL, Sanctuary BC, Shoubridge EA: 1H NMR characterization of normal human cerebrospinal fluid and the detection of methylmalonic acid in a vitamin B12 deficient patient. NMR Biomed. 1991 Aug;4(4):192-200. [PubMed Link Image]
Biofluid CSF
Value 623.6 +/- 71.6 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 518.0 +/- 81.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 425.0 +/- 70.5 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 432 +/- 204 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Saliva
Value >10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 118.96 +/- 89.94 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 36.8 (14.5-59.2) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 20.0 (9.0-33.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gatti R, Gioia MG: Liquid chromatographic fluorescence determination of amino acids in plasma and urine after derivatization with phanquinone. Biomed Chromatogr. 2008 Feb;22(2):207-13. [PubMed Link Image]
Biofluid Urine
Value 496 +/- 8 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Blood
Value 476.0 (455.0-498.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Acute seizures
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 495.0 (477.0-513.0) uM
Age Children:1-13 yrs old
Sex Both
Condition Epilepsy
Comments Juvenile myoclonic epilepsy (JME)
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 611.0 (591.0-630.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Refractory localization-related epilepsy (RLE)
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 650.0 +/- 98.0 uM
Age Adult:>18 yrs old
Sex Male
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid Blood
Value 673.0 +/- 96.0 uM
Age Adult:>18 yrs old
Sex Female
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid Blood
Value 228.34 +/- 12.00 uM
Age Elderly:>65 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Blood
Value 900.0 (700.0-1100.0) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid CSF
Value 254.0 (152.0-356.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. [PubMed Link Image]
Biofluid CSF
Value 1875.3 +/- 285.8 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Acute Lymphoblastic Leukemia (ALL) with Central Nervous System (CNS) disease
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 1061.0 +/- 230.2 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 1146.6 +/- 10.6 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Urine
Value 1.17 +/- 0.49 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Urine
Value 41.6 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Abnormal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
Epilepsy
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Leukemia
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Schizophrenia
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
Phenylacetate Metabolism SMP00126 Link Image map00360 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
Transcription/Translation SMP00019 Link Image
Urea Cycle SMP00059 Link Image map00330 Link Image
General References
  1. Szebenyi G, Morfini GA, Babcock A, Gould M, Selkoe K, Stenoien DL, Young M, Faber PW, MacDonald ME, McPhaul MJ, Brady ST: Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport. Neuron. 2003 Sep 25;40(1):41-52. [PubMed Link Image]
  2. Wada A, Yoshida R, Oda K, Fukuba E, Uchida N, Kitagaki H: Acute encephalopathy associated with intravenous immunoglobulin therapy. AJNR Am J Neuroradiol. 2005 Oct;26(9):2311-5. [PubMed Link Image]
  3. Pennisi P, Gavrilova O, Setser-Portas J, Jou W, Santopietro S, Clemmons D, Yakar S, LeRoith D: Recombinant human insulin-like growth factor-I treatment inhibits gluconeogenesis in a transgenic mouse model of type 2 diabetes mellitus. Endocrinology. 2006 Jun;147(6):2619-30. Epub 2006 Mar 2. [PubMed Link Image]
  4. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
  5. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
  6. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
  7. Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
  8. Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. [PubMed Link Image]
  9. Avila J, Barbaro B, Gangemi A, Romagnoli T, Kuechle J, Hansen M, Shapiro J, Testa G, Sankary H, Benedetti E, Lakey J, Oberholzer J: Intra-ductal glutamine administration reduces oxidative injury during human pancreatic islet isolation. Am J Transplant. 2005 Dec;5(12):2830-7. [PubMed Link Image]
  10. Cooper AJ: Ammonia metabolism in normal and portacaval-shunted rats. Adv Exp Med Biol. 1990;272:23-46. [PubMed Link Image]
  11. Melis GC, Boelens PG, van der Sijp JR, Popovici T, De Bandt JP, Cynober L, van Leeuwen PA: The feeding route (enteral or parenteral) affects the plasma response of the dipetide Ala-Gln and the amino acids glutamine, citrulline and arginine, with the administration of Ala-Gln in preoperative patients. Br J Nutr. 2005 Jul;94(1):19-26. [PubMed Link Image]
  12. Choudry HA, Pan M, Karinch AM, Souba WW: Branched-chain amino acid-enriched nutritional support in surgical and cancer patients. J Nutr. 2006 Jan;136(1 Suppl):314S-8S. [PubMed Link Image]
  13. Commodari F, Arnold DL, Sanctuary BC, Shoubridge EA: 1H NMR characterization of normal human cerebrospinal fluid and the detection of methylmalonic acid in a vitamin B12 deficient patient. NMR Biomed. 1991 Aug;4(4):192-200. [PubMed Link Image]
  14. Frayn KN, Khan K, Coppack SW, Elia M: Amino acid metabolism in human subcutaneous adipose tissue in vivo. Clin Sci (Lond). 1991 May;80(5):471-4. [PubMed Link Image]
  15. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  16. Coeffier M, Miralles-Barrachina O, Le Pessot F, Lalaude O, Daveau M, Lavoinne A, Lerebours E, Dechelotte P: Influence of glutamine on cytokine production by human gut in vitro. Cytokine. 2001 Feb 7;13(3):148-54. [PubMed Link Image]
  17. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. [PubMed Link Image]
  18. Rutten EP, Engelen MP, Wouters EF, Schols AM, Deutz NE: Metabolic effects of glutamine and glutamate ingestion in healthy subjects and in persons with chronic obstructive pulmonary disease. Am J Clin Nutr. 2006 Jan;83(1):115-23. [PubMed Link Image]
  19. van der Hulst RR, von Meyenfeldt MF, Deutz NE, Soeters PB: Glutamine extraction by the gut is reduced in depleted [corrected] patients with gastrointestinal cancer. Ann Surg. 1997 Jan;225(1):112-21. [PubMed Link Image]
  20. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
  2. Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1
  3. Amidophosphoribosyltransferase precursor
  4. Kynurenine--oxoglutarate transaminase 1
  5. Glutaminyl-tRNA synthetase
  6. Asparagine synthetase [glutamine-hydrolyzing]
  7. GMP synthase [glutamine-hydrolyzing]
  8. Protein-glutamine gamma-glutamyltransferase E precursor
  9. Protein-glutamine gamma-glutamyltransferase 2
  10. Glutamine synthetase
  11. Coagulation factor XIII A chain precursor
  12. Glutaminase liver isoform, mitochondrial precursor
  13. CTP synthase 1
  14. Protein-glutamine gamma-glutamyltransferase 5
  15. Glutaminase kidney isoform, mitochondrial precursor
  16. Protein-glutamine gamma-glutamyltransferase K
  17. Protein-glutamine gamma-glutamyltransferase 6
  18. Phosphoribosylformylglycinamidine synthase
  19. Probable glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial precursor
  20. Neutral amino acid transporter B(0)
  21. Large neutral amino acids transporter small subunit 2
  22. L-glutaminase
  23. System N amino acid transporter 1
  24. Glutamine-dependent NAD(+) synthetase
  25. CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
  26. cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase
  27. cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase
  28. Glutamine synthetase
  29. Putative uncharacterized protein GFPT1
  30. cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
  31. cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K (Cysteine conjugate-beta lyase
  32. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
  33. Glutamyl-tRNA(Gln) amidotransferase subunit A homolog
Enzyme 1 [top]
Enzyme 1 ID 5446
Enzyme 1 Name Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2
Enzyme 1 Synonyms
  1. Hexosephosphate aminotransferase 2
  2. D-fructose-6- phosphate amidotransferase 2
  3. GFAT 2
  4. GFAT2
Enzyme 1 Gene Name GFPT2
Enzyme 1 Protein Sequence >Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 2 
MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKR
GKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHN
GIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEG
AFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMK
RLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSAS
DDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDH
LKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFF
ISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYT
SQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRS
LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCF
AKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFH
LAVLRGYDVDFPRNLAKSVTVE
Enzyme 1 Number of Residues 682
Enzyme 1 Molecular Weight 76932
Enzyme 1 Theoretical pI 7.40
Enzyme 1 GO Classification
Function
  • binding
  • carbohydrate binding
  • catalytic activity
  • glutamine-fructose-6-phosphate transaminase (isomerizing) activity
  • sugar binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • carbohydrate biosynthesis
  • carbohydrate metabolism
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Cell wall/membrane/envelope biogenesis
Enzyme 1 Specific Function Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4239883 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O94808 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GFPT2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2049 bp 
ATGTGCGGAATCTTTGCCTACATGAACTACAGAGTCCCCCGGACGAGGAAGGAGATCTTC
GAAACCCTCATCAAGGGCCTGCAGCGGCTGGAGTACAGAGGCTACGACTCGGCAGGTGTG
GCGATCGATGGGAATAATCACGAAGTCAAAGAAAGACACATTCAGCTGGTCAAGAAAAGG
GGGAAAGTCAAGGCTCTCGATGAAGAACTTTACAAACAAGACAGCATGGACTTAAAAGTG
GAGTTTGAGACACACTTCGGCATTGCCCACACGCGCTGGGCCACCCACGGGGTCCCCAGT
GCTGTCAACAGCCACCCTCAGCGCTCAGACAAAGGCAACGAATTTGTTGTCATCCACAAT
GGGATCATCACAAATTACAAAGATCTGAGGAAATTTCTGGAAAGCAAAGGCTACGAGTTT
GAGTCAGAAACAGATACAGAGACCATCGCCAAGCTGATTAAATATGTGTTCGACAACAGA
GAAACTGAGGACATTACGTTTTCAACGTTGGTCGAGAGAGTCATTCAGCAGTTGGAAGGT
GCATTCGCGCTGGTTTTCAAGAGTGTCCACTACCCAGGAGAAGCCGTTGCCACACGGAGA
GGCAGCCCCCTGCTCATCGGAGTCCGGAGCAAATACAAGCTCTCCACAGAACAGATCCCT
ATCTTATACAGGACGTGCACTCTGGAGAATGTGAAGAATATCTGTAAGACACGGATGAAG
AGGCTGGACAGCTCCGCCTGCCTGCATGCTGTGGGCGACAAGGCCGTGGAATTCTTCTTT
GCTTCTGATGCAAGCGCTATCATAGAGCACACCAACCGGGTCATCTTCCTGGAGGACGAT
GACATCGCCGCAGTGGCTGATGGGAAACTCTCCATTCACCGGGTCAAGCGCTCGGCCAGT
GATGACCCATCTCGAGCCATCCAGACCTTGCAGATGGAACTGCAGCAAATCATGAAAGGT
AACTTCAGTGCGTTTATGCAGAAGGAGATCTTCGAACAGCCAGAATCAGTTTTCAATACT
ATGAGAGGTCGGGTGAATTTTGAAACCAACACAGTGCTCCTGGGTGGCTTGAAGGACCAC
TTGAAGGAGATTCGACGATGCCGACGGCTCATCGTGATTGGCTGTGGAACCAGCTACCAC
GCTGCCGTGGCTACGCGGCAAGTTTTGGAGGAACTGACTGAGCTTCCTGTGATGGTTGAA
CTTGCTAGTGATTTTCTGGACAGGAACACACCTGTGTTCAGGGATGACGTTTGCTTTTTC
ATCAGCCAGTCAGGCGAGACCGCGGACACCCTCCTGGCGCTGCGCTACTGTAAGGACCGC
GGCGCTCTCACCGTGGGCGTCACCAACACCGTGGGCAGCTCCATCTCTCGCGAGACCGAC
TGCGGCGTCCACATCAACGCAGGGCCGGAGATCGGCGTGGCCAGCACCAAGGCTTATACC
AGTCAGTTCATCTCTCTGGTGATGTTTGGTTTGATGATGTCTGAAGACCGAATTTCACTA
CAAAACAGGAGGCAAGAGATCATCCGTGGCTTGAGATCTTTACCTGAGCTGATCAAGGAA
GTGCTGTCTCTGGAGGAGAAGATCCACGACTTGGCCCTGGAGCTCTACACGCAGAGATCG
CTGCTGGTGATGGGGCGGGGCTACAACTATGCCACCTGCCTGGAAGGAGCCCTGAAAATT
AAAGAGATAACCTACATGCACTCAGAAGGCATCCTGGCTGGGGAGCTGAAGCACGGGCCC
CTGGCACTGATTGACAAGCAGATGCCCGTCATCATGGTCATTATGAAGGATCCTTGCTTC
GCCAAATGCCAGAACGCCCTGCAGCAAGTCACGGCCCGCCAGGGTCGCCCCATTATACTG
TGCTCCAAGGACGATACTGAAAGTTCCAAGTTTGCGTATAAGACAATTGAGCTGCCCCAC
ACTGTGGACTGCCTCCAGGGCATCCTGAGCGTGATTCCGCTGCAGCTGCTGTCCTTCCAC
CTGGCTGTTCTCCGAGGATATGACGTTGACTTCCCCAGAAATCTGGCCAAGTCTGTAACT
GTGGAATGA
Enzyme 1 GenBank Gene ID AB016789 Link Image
Enzyme 1 GeneCard ID GFPT2 Link Image
Enzyme 1 GenAtlas ID GFPT2 Link Image
Enzyme 1 HGNC ID HGNC:4242 Link Image
Enzyme 1 Chromosome Location 5
Enzyme 1 Locus 5q34-q35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Oki T, Yamazaki K, Kuromitsu J, Okada M, Tanaka I: cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-phosphate amidotransferase (GFAT2) in human and mouse. Genomics. 1999 Apr 15;57(2):227-34. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5448
Enzyme 2 Name Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1
Enzyme 2 Synonyms
  1. Hexosephosphate aminotransferase 1
  2. D-fructose-6- phosphate amidotransferase 1
  3. GFAT 1
  4. GFAT1
Enzyme 2 Gene Name GFPT1
Enzyme 2 Protein Sequence >Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1 
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLI
KKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIV
IHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQ
LEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSKFTRW
GSQGERGKDKKGSCNLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVA
AVVDGRLSIHRIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRG
RVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELAS
DFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV
HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLS
MDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLAL
VDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVD
CLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE
Enzyme 2 Number of Residues 699
Enzyme 2 Molecular Weight 78808
Enzyme 2 Theoretical pI 7.11
Enzyme 2 GO Classification
Function
  • binding
  • carbohydrate binding
  • catalytic activity
  • glutamine-fructose-6-phosphate transaminase (isomerizing) activity
  • sugar binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • carbohydrate biosynthesis
  • carbohydrate metabolism
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Cell wall/membrane/envelope biogenesis
Enzyme 2 Specific Function Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins
Enzyme 2 Pathways
Enzyme 2 Reactions
  • L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 183082 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q06210 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GFPT1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2046 bp 
ATGTGTGGTATATTTGCTTACTTAAACTACCATGTTCCTCGAACGAGACGAGAAATCCTG
GAGACCCTAATCAAAGGCCTTCAGAGACTGGAGTACAGAGGATATGATTCTGCTGGTGTG
GGATTTGATGGAGGCAATGATAAAGATTGGGAAGCCAATGCCTGCAAAACCCAGCTTATT
AAGAAGAAAGGAAAAGTTAAGGCACTGGATGAAGAAGTTCACAAGCAACAAGATATGGAT
TTGGATATAGAATTTGATGTACACCTTGGAATAGCTCATACCCGTTGGGCAACACATGGA
GAACCCAGTCCTGTCAATAGCCACCCCCAGCGCTCTGATAAAAATAATGAATTTATCGTT
ATTCACAATGGAATCATCACCAACTACAAAGACTTGAAAAAGTTTTTGGAAAGCAAAGGC
TATGACTTCGAATCTGAAACAGACACAGAGACAATTGCCAAGCTCGTTAAGTATATGTAT
GACAATCGGGAAAGTCAAGATACCAGCTTTACTACCTTGGTGGAGAGAGTTATCCAACAA
TTGGAAGGTGCTTTTGCACTTGTGTTTAAAAGTGTTCATTTTCCCGGGCAAGCAGTTGGC
ACAAGGCGAGGTAGCCCTCTGTTGATTGGTGTACGGAGTGAACATAAACTTTCTACTGAT
CACATTCCTATACTCTACAGAACAGGCAAAGACAAGAAAGGAAGCTGCAATCTCTCTCGT
GTGGACAGCACAACCTGCCTTTTCCCGGTGGAAGAAAAAGCAGTGGAGTATTACTTTGCT
TCTGATGCAAGTGCTGTCATAGAACACACCAATCGCGTCATCTTTCTGGAAGATGATGAT
GTTGCAGCAGTAGTGGATGGACGTCTTTCTATCCATCGAATTAAACGAACTGCAGGAGAT
CACCCCGGACGAGCTGTGCAAACACTCCAGATGGAACTCCAGCAGATCATGAAGGGCAAC
TTCAGTTCATTTATGCAGAAGGAAATATTTGAGCAGCCAGAGTCTGTCGTGAACACAATG
AGAGGAAGAGTCAACTTTGATGACTATACTGTGAATTTGGGTGGTTTGAAGGATCACATA
AAGGAGATCCAGAGATGCCGGCGTTTGATTCTTATTGCTTGTGGAACAAGTTACCATGCT
GGTGTAGCAACACGTCAAGTTCTTGAGGAGCTGACTGAGTTGCCTGTGATGGTGGAACTA
GCAAGTGACTTCCTGGACAGAAACACACCAGTCTTTCGAGATGATGTTTGCTTTTTCCTT
AGTCAATCAGGTGAGACAGCAGATACTTTGATGGGTCTTCGTTACTGTAAGGAGAGAGGA
GCTTTAACTGTGGGGATCACAAACACAGTTGGCAGTTCCATATCACGGGAGACAGATTGT
GGAGTTCATATTAATGCTGGTCCTGAGATTGGTGTGGCCAGTACAAAGGCTTATACCAGC
CAGTTTGTATCCCTTGTGATGTTTGCCCTTATGATGTGTGATGATCGGATCTCCATGCAA
GAAAGACGCAAAGAGATCATGCTTGGATTGAAACGGCTGCCTGATTTGATTAAGGAAGTA
CTGAGCATGGATGACGAAATTCAGAAACTAGCAACAGAACTTTATCATCAGAAGTCAGTT
CTGATAATGGGACGAGGCTATCATTATGCTACTTGTCTTGAAGGGGCACTGAAAATCAAA
GAAATTACTTATATGCACTCTGAAGGCATCCTTGCTGGTGAATTGAAACATGGCCCTCTG
GCTTTGGTGGATAAATTGATGCCTGTGATCATGATCATCATGAGAGATCACACTTATGCC
AAGTGTCAGAATGCTCTTCAGCAAGTGGTTGCTCGGCAGGGGCGGCCTGTGGTAATTTGT
GATAAGGAGGATACTGAGACCATTAAGAACACAAAAAGAACGATCAAGGTGCCCCACTCA
GTGGACTGCTTGCAGGGCATTCTCAGCGTGATCCCTTTACAGTTGCTGGCTTTCCACCTT
GCTGTGCTGAGAGGCTATGATGTTGATTTCCCACGGAATCTTGCCAAATCTGTGACTGTA
GAGTGA
Enzyme 2 GenBank Gene ID M90516 Link Image
Enzyme 2 GeneCard ID GFPT1 Link Image
Enzyme 2 GenAtlas ID GFPT1 Link Image
Enzyme 2 HGNC ID HGNC:4241 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. McKnight GL, Mudri SL, Mathewes SL, Traxinger RR, Marshall S, Sheppard PO, O'Hara PJ: Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase. J Biol Chem. 1992 Dec 15;267(35):25208-12. [PubMed Link Image]
  2. DeHaven JE, Robinson KA, Nelson BA, Buse MG: A novel variant of glutamine: fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle. Diabetes. 2001 Nov;50(11):2419-24. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5567
Enzyme 3 Name Amidophosphoribosyltransferase precursor
Enzyme 3 Synonyms
  1. Glutamine phosphoribosylpyrophosphate amidotransferase
  2. ATASE
  3. GPAT
Enzyme 3 Gene Name PPAT
Enzyme 3 Protein Sequence >Amidophosphoribosyltransferase precursor 
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Enzyme 3 Number of Residues 517
Enzyme 3 Molecular Weight 57400
Enzyme 3 Theoretical pI 6.74
Enzyme 3 GO Classification
Function
  • amidophosphoribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • physiological process
  • purine base biosynthesis
  • purine base metabolism
Component
—
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 219459 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q06203 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PUR1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1554 bp 
ATGGAGCTGGAGGAGTTGGGGATCCGAGAGGAATGTGGCGTGTTCGGGTGCATCGCCTCA
GGAGAGTGGCCCACGCAGCTGGATGTACCGCATGTGATCACTCTGGGACTCGTGGGGCTG
CAGCACCGGGGTCAGGAGAGTGCTGGTATTGTGACTAGTGATGGGAGTTCGGTGCCAACA
TTCAAATCACACAAGGGAATGGGTCTTGTAAATCACGTCTTTACTGAAGACAATTTGAAA
AAATTATATGTTTCAAATCTTGGAATTGGACACACCAGGTATGCCACCACAGGAAAATGT
GAACTAGAAAATTGTCAGCCCTTCGTTGTTGAAACACTTCATGGGAAGATAGCTGTGGCA
CATAATGGCGAATTGGTAAATGCTGCTCGATTAAGGAAAAAGCTTCTGCGTCATGGTATT
GGTCTGTCTACAAGTTCTGATAGTGAAATGATTACCCAGTTACTGGCGTATACCCCTCCT
CAGGAACAAGATGACACCCCAGACTGGGTAGCCAGGATTAAAAACTTGATGAAGGAAGCA
CCCACAGCATACTCCCTGCTTATAATGCACAGAGATGTTATTTATGCAGTACGAGATCCT
TATGGAAATCGTCCCTTATGCATTGGTCGTCTTATTCCAGTGTCTGATATAAATGACAAA
GAGAAAAAAACATCAGAAACAGAAGGATGGGTGGTGTCTTCAGAATCTTGTAGCTTCTTA
TCTATTGGTGCAAGATATTACCGTGAAGTCTTGCCTGGAGAAATTGTGGAAATATCCAGA
CACAATGTCCAAACTCTTGATATTATATCAAGGTCTGAAGGAAACCCAGTGGCTTTTTGT
ATCTTTGAATATGTTTATTTTGCAAGACCAGACAGTATGTTCGAAGACCAAATGGTTTAT
ACAGTAAGATACCGTTGTGGCCAGCAGCTAGCGATTGAAGCACCTGTGGATGCAGATTTG
GTTAGCACTGTTCCAGAATCTGCTACGCCTGCTGCTCTTGCTTACGCAGGAAAGTGTGGA
CTTCCATATGTGGAGGTGCTGTGTAAAAACCGGTATGTAGGGAGAACCTTCATTCAGCCA
AACATGAGGTTAAGACAACTTGGTGTTGCAAAAAAATTTGGAGTATTGTCAGACAACTTT
AAAGGCAAAAGAATTGTTCTTGTAGATGATTCAATTGTCAGAGGCAATACCATCTCACCT
ATAATAAAACTGCTCAAAGAATCTGGTGCAAAAGAGGTACACATTCGAGTAGCTTCACCA
CCAATTAAATATCCATGCTTCATGGGAATAAACATTCCTACAAAAGAAGAGCTCATTGCC
AATAAACCAGAATTTGATCACCTTGCAGAATATCTAGGAGCAAACAGTGTTGTGTATCTG
TCAGTAGAAGGACTGGTTTCATCTGTACAAGAAGGGATAAAGTTTAAAAAACAGAAAGAG
AAAAAGCACGATATTATGATCCAAGAAAATGGAAATGGTCTGGAATGTTTTGAAAAGAGT
GGTCATTGTACAGCTTGTCTCACTGGAAAATATCCTGTAGAATTAGAATGGTAG
Enzyme 3 GenBank Gene ID D13757 Link Image
Enzyme 3 GeneCard ID PPAT Link Image
Enzyme 3 GenAtlas ID PPAT Link Image
Enzyme 3 HGNC ID HGNC:9238 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Iwahana H, Oka J, Mizusawa N, Kudo E, Ii S, Yoshimoto K, Holmes EW, Itakura M: Molecular cloning of human amidophosphoribosyltransferase. Biochem Biophys Res Commun. 1993 Jan 15;190(1):192-200. [PubMed Link Image]
  2. Brayton KA, Chen Z, Zhou G, Nagy PL, Gavalas A, Trent JM, Deaven LL, Dixon JE, Zalkin H: Two genes for de novo purine nucleotide synthesis on human chromosome 4 are closely linked and divergently transcribed. J Biol Chem. 1994 Feb 18;269(7):5313-21. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5703
Enzyme 4 Name Kynurenine--oxoglutarate transaminase 1
Enzyme 4 Synonyms
  1. Kynurenine-- oxoglutarate transaminase I
  2. Kynurenine aminotransferase I
  3. KATI
  4. Glutamine--phenylpyruvate transaminase
  5. Glutamine transaminase K
  6. GTK
  7. Cysteine-S-conjugate beta-lyase
Enzyme 4 Gene Name CCBL1
Enzyme 4 Protein Sequence >Kynurenine--oxoglutarate transaminase 1 
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
Enzyme 4 Number of Residues 422
Enzyme 4 Molecular Weight 47876
Enzyme 4 Theoretical pI 6.45
Enzyme 4 GO Classification
Function
  • 1-aminocyclopropane-1-carboxylate synthase activity
  • carbon-sulfur lyase activity
  • catalytic activity
  • lyase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kinurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta- elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond
Enzyme 4 Pathways
Enzyme 4 Reactions
  • RS-CH2-CH(NH3+)COO- = RSH + ammonia + pyruvate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 758591 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q16773 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KAT1_HUMAN Link Image
Enzyme 4 PDB ID 1W7N Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1269 bp 
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTCATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
Enzyme 4 GenBank Gene ID X82224 Link Image
Enzyme 4 GeneCard ID CCBL1 Link Image
Enzyme 4 GenAtlas ID CCBL1 Link Image
Enzyme 4 HGNC ID HGNC:1564 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q34.11
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Perry S, Harries H, Scholfield C, Lock T, King L, Gibson G, Goldfarb P: Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase. FEBS Lett. 1995 Mar 6;360(3):277-80. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5852
Enzyme 5 Name Glutaminyl-tRNA synthetase
Enzyme 5 Synonyms
  1. Glutamine--tRNA ligase
  2. GlnRS
Enzyme 5 Gene Name QARS
Enzyme 5 Protein Sequence >Glutaminyl-tRNA synthetase 
MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLA
SRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPE
QIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPK
LEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKT
PGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFL
RFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQ
RGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRV
KYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV
QWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVG
VTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADET
KGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVES
LEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASL
HVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV
Enzyme 5 Number of Residues 775
Enzyme 5 Molecular Weight 87800
Enzyme 5 Theoretical pI 7.16
Enzyme 5 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • glutamate-tRNA ligase activity
  • glutamine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • glutamyl-tRNA aminoacylation
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
—
Enzyme 5 General Function Translation, ribosomal structure and biogenesis
Enzyme 5 Specific Function ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 558586 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P47897 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SYQ_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2328 bp 
ATGGCGGCTCTAGACTCCCTGTCGCTCTTCACTAGCCTCGGCCTGAGCGAGCAGAAGGCC
CGCGAGACGCTCAAGAACTCGGCTCTGAGCGCGCAGCTGCGCGAGGCCGCTACTCAGGCT
CAGCAGACCCTGGGTTCCACCATTGACAAAGCTACCGGGATCCTGTTATATGGCTTGGCC
TCCCGACTCAGGGATACCCGGCGTCTCTCCTTCCTTGTAAGCTACATAGCCAGTAAGAAG
ATCCACACTGAGCCCCAGCTAAGCGCTGCCCTTGAGTATGTGCGGAGTCACCCCTTGGAC
CCCATCGACACTGTGGACTTCGAGCGGGAATGTGGCGTGGGTGTCATTGTGACCCCAGAG
CAGATTGAGGAGGCTGTGGAGGCTGCTATTAACAGGCACCGGCCCCAGCTCCTGGTGGAA
CGTTACCATTTCAACATGGGGCTGCTGATGGGAGAGGCTCGGGCTGTGCTGAAGTGGGCA
GATGGCAAAATGATCAAGAATGAAGTGGACATGCAGGTCCTCCACCTTCTGGGCCCCAAG
TTGGAGGCTGATCTGGAGAAGAAGTTCAAGGTGGCAAAAGCTCGGCTAGAAGAAACAGAC
CGGAGGACGGCAAAGGATGTGGTGGAGAATGGCGAGACTGCTGACCAGACCCTGTCTCTG
ATGGAGCAGCTCCGGGGGGAGGCCCTTAAGTTCCACAAGCCTGGTGAGAACTACAAGACC
CCAGGCTATGTGGTCACTCCACACACCATGAATCTACTAAAGCAGCACCTGGAGATTACT
GGTGGGCAGGTACGTACCCGGTTCCCGCCAGAACCCAATGGAATCCTGCATATTGGACAT
GCCAAAGCCATCAATTTCAACTTTGGCTATGCCAAGGCCAACAATGGCATCTGTTTTCTG
CGTTTTGATGACACCAACCCTGAGAAGGAGGAAGCAAAGTTCTTCACGGCCATCTGTGAC
ATGGTAGCCTGGCTAGGCTACACACCTTACAAAGTCACATATGCGTCTGACTATTTTGAC
CAGCTATATGCGTGGGCTGTGGAGCTCATCCGCAGGGGTCTGGCTTATGTGTGCCACCAG
CGAGGAGAGGAGCTCAAAGGCCATAATACTCTGCCTTCACCCTGGAGAGACCGTCCCATG
GAGGAGTCACTGCTGCTCTTTGAGGCAATGCGCAAGGGCAAGTTTTCAGAGGGCGAGGCC
ACACTACGGATGAAGCTGGTGATGGAGGATGGCAAGATGGACCCTGTAGCCTATCGAGTC
AAGTATACACCACACCACCGCACAGGGGACAAATGGTGCATCTATCCCACCTACGACTAC
ACACACTGCCTCTGTGACTCCATCGAGCACATCACTCACTCACTCTGCACCAAGGAATTC
CAGGCCCGACGCTCTTCCTACTTCTGGCTTTGCAATGCACTGGACGTCTATTGCCCTGTG
CAGTGGGAGTATGGCCGCCTCAACCTGCACTATGCTGTTGTCTCTAAGAGGAAGATCCTC
CAGCTTGTAGCAACTGGTGCTGTGCGGGACTGGGATGACCCACGGCTCTTTACACTCACG
GCCCTGCGACGGCGGGGCTTCCCACCTGAGGCCATCAACAACTTCTGTGCCCGGGTGGGA
GTGACTGTGGCACAAACCACAATGGAGCCACATCTTCTAGAAGCCTGTGTGCGTGATGTG
CTGAATGACACAGCCCCACGAGCCATGGCTGTGCTGGAGTCACTACGGGTCATCATCACC
AACTTTCCTGCTGCCAAGTCCTTGGACATCCAGGTGCCCAACTTCCCAGCTGATGAGACC
AAAGGCTTCCATCAGGTTCCCTTTGCACCCATTGTCTTCATTGAGAGGACTGACTTCAAG
GAGGAGCCAGAGCCAGGATTTAAGCGCCTGGCTTGGGGCCAGCCTGTGGGCCTGAGGCAT
ACAGGCTACGTCATTGAGCTGCAGCATGTTGTCAAGGGCCCCAGTGGTTGTGTAGAGAGT
CTGGAGGTGACCTGCAGACGGGCAGATGCTGGAGAGAAGCCAAAGGCCTTTATTCACTGG
GTGTCACAGCCTTTGATGTGTGAGGTTCGCCTCTATGAGCGACTATTCCAGCACAAGAAC
CCTGAAGATCCTACTGAGGTGCCTGGTGGATTTTTAAGTGACCTGAACCTGGCATCACTA
CACGTGGTGGATGCAGCATTAGTGGACTGCTCTGTGGCCCTGGCAAAACCCTTCGACAAG
TTCCAGTTTGAGCGTCTTGGATATTTCTCCGTGGATCCAGACAGCCATCAGGGAAAGCTT
GTCTTTAACCGAACTGTCACACTGAAGGAAGACCCAGGAAAGGTGTGA
Enzyme 5 GenBank Gene ID X76013 Link Image
Enzyme 5 GeneCard ID QARS Link Image
Enzyme 5 GenAtlas ID QARS Link Image
Enzyme 5 HGNC ID HGNC:9751 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3p21.3-p21.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M: Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8670-4. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5855
Enzyme 6 Name Asparagine synthetase [glutamine-hydrolyzing]
Enzyme 6 Synonyms
  1. Glutamine- dependent asparagine synthetase
  2. Cell cycle control protein TS11
Enzyme 6 Gene Name ASNS
Enzyme 6 Protein Sequence >Asparagine synthetase [glutamine-hydrolyzing] 
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA
Enzyme 6 Number of Residues 561
Enzyme 6 Molecular Weight 64371
Enzyme 6 Theoretical pI 6.85
Enzyme 6 GO Classification
Function
  • asparagine synthase (glutamine-hydrolyzing) activity
  • asparagine synthase (glutamine-hydrolyzing) activity
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • asparagine biosynthesis
  • asparagine metabolism
  • aspartate family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Amino acid transport and metabolism
Enzyme 6 Specific Function ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 179100 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P08243 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ASNS_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1686 bp 
ATGTGTGGCATTTGGGCGCTGTTTGGCAGTGATGATTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGAGGTCCAGATGCATTCCGTTTTGAGAATGTCAATGGATAC
ACCAACTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCCGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCGTATTTGTGGCTCTGTTACAATGGTGAAATCTACAAC
CATAAGAAGATGCAACAGCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAGATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAGCAAACAATTTGTATGTTGGATGGTGTG
TTTGCATTTGTTTTACTGGATACTGCCAATAAGAAAGTGTTCCTGGGTAGAGATACATAT
GGAGTCAGACCTTTGTTTAAAGCAATGACAGAAGATGGATTTTTGGCTGTATGTTCAGAA
GCTAAAGGTCTTGTTACATTGAAGCACTCCGCGACTCCCTTTTTAAAAGTGGAGCCTTTT
CTTCCTGGACACTATGAAGTTTTGGATTTAAAGCCAAATGGCAAAGTTGCATCCGTGGAA
ATGGTTAAATATCATCACTGTCGGGATGTACCCCTGCACGCCCTCTATGACAATGTGGAG
AAACTCTTTCCAGGTTTTGAGATAGAAACTGTGAAGAACAACCTCAGGATCCTTTTTAAT
AATGCTGTAAAGAAACGTTTGATGACAGACAGAAGGATTGGCTGCCTTTTATCAGGGGGC
TTGGACTCCAGCTTGGTTGCTGCCACTCTGTTGAAGCAGCTGAAAGAAGCCCAAGTACAG
TATCCTCTCCAGACATTTGCAATTGGCATGGAAGACAGCCCCGATTTACTGGCTGCTAGA
AAGGTGGCAGATCATATTGGAAGTGAACATTATGAAGTCCTTTTTAACTCTGAGGAAGGC
ATTCAGGCTCTGGATGAAGTCATATTTTCCTTGGAAACTTATGACATTACAACAGTTCGT
GCTTCAGTAGGTATGTATTTAATTTCCAAGTATATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGATCAGATGAACTTACGCAGGGTTACATATATTTTCACAAGGCT
CCTTCTCCTGAAAAAGCCGAGGAGGAGAGTGAGAGGCTTCTGAGGGAACTCTATTTGTTT
GATGTTCTCCGCGCAGATCGAACTACTGCTGCCCATGGTCTTGAACTGAGAGTCCCATTT
CTAGATCATCGATTTTTTTCCTATTACTTGTCTCTGCCACCAGAAATGAGAATTCCAAAG
AATGGGATAGAAAAACATCTCCTGAGAGAGACGTTTGAGGATTCCAATCTGATACCCAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACTTCAGTTAAGAATTCC
TGGTTTAAGATTTTACAGGAATACGTTGAACATCAGGTTGATGATGCAATGATGGCAAAT
GCAGCCCAGAAATTTCCCTTCAATACTCCTAAAACCAAAGAAGGATATTACTACCGTCAA
GTCTTTGAACGCCATTACCCAGGCCGGGCTGACTGGCTGAGCCATTACTGGATGCCCAAG
TGGATCAATGCCACTGACCCTTCTGCCCGCACGCTGACCCACTACAAGTCAGCTGTCAAA
GCTTAG
Enzyme 6 GenBank Gene ID M27396 Link Image
Enzyme 6 GeneCard ID ASNS Link Image
Enzyme 6 GenAtlas ID ASNS Link Image
Enzyme 6 HGNC ID HGNC:753 Link Image
Enzyme 6 Chromosome Location 7
Enzyme 6 Locus 7q21.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. [PubMed Link Image]
  2. Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Greco A, Ittmann M, Basilico C: Molecular cloning of a gene that is necessary for G1 progression in mammalian cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1565-9. [PubMed Link Image]
  5. Greco A, Gong SS, Ittmann M, Basilico C: Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase. Mol Cell Biol. 1989 Jun;9(6):2350-9. [PubMed Link Image]
  6. Van Heeke G, Schuster SM: Expression of human asparagine synthetase in Escherichia coli. J Biol Chem. 1989 Apr 5;264(10):5503-9. [PubMed Link Image]
  7. Van Heeke G, Schuster SM: The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J Biol Chem. 1989 Nov 25;264(33):19475-7. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5864
Enzyme 7 Name GMP synthase [glutamine-hydrolyzing]
Enzyme 7 Synonyms
  1. Glutamine amidotransferase
  2. GMP synthetase
Enzyme 7 Gene Name GMPS
Enzyme 7 Protein Sequence >GMP synthase [glutamine-hydrolyzing] 
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 7 Number of Residues 693
Enzyme 7 Molecular Weight 76716
Enzyme 7 Theoretical pI 6.86
Enzyme 7 GO Classification
Function
  • ATP binding
  • GMP synthase (glutamine-hydrolyzing) activity
  • GMP synthase (glutamine-hydrolyzing) activity
  • adenyl nucleotide binding
  • binding
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • molecular function unknown
  • nucleotide binding
  • purine nucleotide binding
Process
  • GMP biosynthesis
  • amino acid and derivative metabolism
  • amino acid metabolism
  • biosynthesis
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 595410 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P49915 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GUAA_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2082 bp 
ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA
Enzyme 7 GenBank Gene ID U10860 Link Image
Enzyme 7 GeneCard ID GMPS Link Image
Enzyme 7 GenAtlas ID GMPS Link Image
Enzyme 7 HGNC ID HGNC:4378 Link Image
Enzyme 7 Chromosome Location 3
Enzyme 7 Locus 3q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hirst M, Haliday E, Nakamura J, Lou L: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J Biol Chem. 1994 Sep 23;269(38):23830-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5938
Enzyme 8 Name Protein-glutamine gamma-glutamyltransferase E precursor
Enzyme 8 Synonyms
  1. TGase E
  2. TGE
  3. TG(E
  4. Transglutaminase-3[Contains: Protein- glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
  5. Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain]
Enzyme 8 Gene Name TGM3
Enzyme 8 Protein Sequence >Protein-glutamine gamma-glutamyltransferase E precursor 
MAALGVQSINWQTAFNRQAHHTDKFSSQELILRRGQNFQVLMIMNKGLGSNERLEFIVST
GPYPSESAMTKAVFPLSNGSSGGWSAVLQASNGNTLTISISSPASAPIGRYTMALQIFSQ
GGISSVKLGTFILLFNPWLNVDSVFMGNHAEREEYVQEDAGIIFVGSTNRIGMIGWNFGQ
FEEDILSICLSILDRSLNFRRDAATDVASRNDPKYVGRVLSAMINSNDDNGVLAGNWSGT
YTGGRDPRSWNGSVEILKNWKKSGFSPVRYGQCWVFAGTLNTALRSLGIPSRVITNFNSA
HDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEGWFVRSDLGPSYGGWQVLDATPQER
SQGVFQCGPASVIGVREGDVQLNFDMPFIFAEVNADRITWLYDNTTGKQWKNSVNSHTIG
RYISTKAVGSNARMDVTDKYKYPEGSDQERQVFQKALGKLKPNTPFAATSSMGLETEEQE
PSIIGKLKVAGMLAVGKEVNLVLLLKNLSRDTKTVTVNMTAWTIIYNGTLVHEVWKDSAT
MSLDPEEEAEHPIKISYAQYEKYLKSDNMIRITAVCKVPDESEVVVERDIILDNPTLTLE
VLNEARVRKPVNVQMLFSNPLDEPVRDCVLMVEGSGLLLGNLKIDVPTLGPKEGSRVRFD
ILPSRSGTKQLLADFSCNKFPAIKAMLSIDVAE
Enzyme 8 Number of Residues 693
Enzyme 8 Molecular Weight 76633
Enzyme 8 Theoretical pI 5.60
Enzyme 8 GO Classification
Function
—
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • peptide cross-linking
  • physiological process
  • protein modification
Component
—
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. It is responsible for the later stages of cell envelope formation in the epidermis and the hair follicle
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 307504 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q08188 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name TGM3_HUMAN Link Image
Enzyme 8 PDB ID 1SGX Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2082 bp 
ATGGCTGCTCTAGGAGTCCAGAGTATCAACTGGCAGAAGGCCTTCAACCGACAAGCGCAT
CACACAGACAAGTTCTCCAGCCAGGAGCTCATCTTGCGGAGAGGCCAAAACTTCCAGGTC
TTAATGATCATGAACAAAGGCCTTGGCTCTAACGAAAGACTGGAGTTCATTGACACCACA
GGGCCTTACCCCTCAGAGTCGGCCATGACGAAGGCTGTGTTTCCACTCTCCAATGGCAGT
AGTGGTGGCTGGAGTGCGGTGCTTCAGGCCAGCAATGGCAATACTCTGACTATCAGCATC
TCCAGTCCTGCCAGCGCACCCATAGGACGGTACACAATGGCCCTCCAGATCTTCTCCCAG
GGCGGCATCTCCTCTGTGAAACTTGGGACGTTCATACTGCTTTTTAACCCCTGGCTGAAT
GTGGATAGCGTCTTTATGGGTAACCATGCTGAGAGAGAAGAGTATGTTCAGGAAGATGCC
GGCATCATCTTTGTGGGAAGCACAAACCGAATTGGCATGATTGGCTGGAACTTTGGACAG
TTTGAAGAAGACATTCTCAGCATCTGCCTCTCAATCTTGGATAGGAGTCTGAATTTCCGC
CGTGACGCTGCTACTGATGTGGCCAGCAGAAATGACCCCAAATACGTTGGCCGGGTGCTG
AGTGCCATGATCAATAGCAATGATGACAATGGTGTGCTTGCTGGGAATTGGAGCGGCACT
TACACCGGTGGCCGGGACCCAAGGAGCTGGGACGGCAGCGTGGAGATCCTCAAAAATTGG
AAAAAATCTGGCTTCAGCCCAGTCCGATATGGCCAGTGCTGGGTCTTTGCTGGGACCCTC
AACACAGCGCTGCGGTCTTTGGGGATTCCTTCCCGGGTGATCACCAACTTCAACTCAGCT
CATGACACAGACCGAAATCTCAGTGTGGATGTGTACTACGACCCCATGGGAAACCCCCTG
GACAAGGGTAGTGATAGCGTATGGAATTTCCATGTCTGGAATGAAGGCTGGTTTGTGAGG
TCTGACCTGGGCCCCCCGTACGGTGGATGGCAGGTGTTGGATGCTACCCCGCAGGAAAGA
AGCCAAGGGGTGTTCCAGTGCGGCCCCGCTTCGGTCATTGGTGTTCGAGAGGGTGATGTG
CAGCTGAACTTCGACATGCCCTTTATCTTCGCGGAGGTTAATGCCGACCGCATCACCTGG
CTGTACGACAACACCACTGGCAAACAGTGGAAGAATTCCGTGAACAGTCACACCATTGGC
AGGTACATCAGCACCAAGGCGGTGGGCAGCAATGCTCGCATGGACGTCACGGACAAGTAC
AAGTACCCAGAAGGCTCTGACCAGGAAAGACAAGTGTTCCAAAAGGCTTTGGGGAAACTT
AAACCCAACACGCCATTTGCCGCGACGTCTTCGATGGGTTTGGAAACAGAGGAACAGGAG
CCCAGCATCATCGGGAAGCTGAAGGTCGCTGGCATGCTGGCAGTAGGCAAAGAAGTCAAC
CTGGTCCTACTGCTCAAAAACCTGAGCAGGGATACGAAGACAGTGACAGTGAACATGACA
GCCTGGACCATCATCTACAACGGCACGCTTGTACATGAAGTGTGGAAGGACTCTGCCACA
ATGTCCCTGGACCCTGAGGAAGAGGCAGAACATCCCATAAAGATCTCGTACGCTCAGTAT
GAGAGGTACCTGAAGTCAGACAACATGATCCGGATCACAGCGGTGTGCAAGGTCCCAGAT
GAGTCTGAGGTGGTGGTGGAGCGGGACATCATCCTGGACAACCCCACCTTGACCCTGGAG
GTGCTGAACGAGGCTCGTGTGCGGAAGCCTGTGAACGTGCAGATGCTCTTCTCCAATCCA
CTGGATGAGCCGGTGAGGGACTGCGTGCTGATGGTGGAGGGAAGCGGCCTGCTGTTGGGT
AACCTGAAGATCGACGTGCCGACCCTAGGGCCCAAGGAGCGGTCCCGGGTCCGTTTTGAT
ATCCTGCCCTCCCGGAGTGGCACCAAGCAACTGCTCGCCGACTTCTCCTGCAACAAGTTC
CCTGCAATCAAGGCCATGTTGTCCATCGACGTAGCCGAATGA
Enzyme 8 GenBank Gene ID L10386 Link Image
Enzyme 8 GeneCard ID TGM3 Link Image
Enzyme 8 GenAtlas ID TGM3 Link Image
Enzyme 8 HGNC ID HGNC:11779 Link Image
Enzyme 8 Chromosome Location 20
Enzyme 8 Locus 20q11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Kim IG, Gorman JJ, Park SC, Chung SI, Steinert PM: The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse. J Biol Chem. 1993 Jun 15;268(17):12682-90. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5940
Enzyme 9 Name Protein-glutamine gamma-glutamyltransferase 2
Enzyme 9 Synonyms
  1. Tissue transglutaminase
  2. TGase C
  3. TGC
  4. TG(C
  5. Transglutaminase-2
  6. TGase- H
Enzyme 9 Gene Name TGM2
Enzyme 9 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 2 
MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFS
VVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLE
ASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPW
NFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGR
WDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTN
YNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPT
PQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSL
IVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
QSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEK
SVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQK
RKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPLHMG
LHKLVVNFESDKLKAVKGFRNVIIGPA
Enzyme 9 Number of Residues 687
Enzyme 9 Molecular Weight 77330
Enzyme 9 Theoretical pI 4.86
Enzyme 9 GO Classification
Function
—
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • peptide cross-linking
  • physiological process
  • protein modification
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 339521 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P21980 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name TGM2_HUMAN Link Image
Enzyme 9 PDB ID 1KV3 Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2064 bp 
ATGGCCGAGGAGCTGGTCTTAGAGAGGTGTGATCTGGAGCTGGAGACCAATGGCCGAGAC
CACCACACGGCCGACCTGTGCCGGGAGAAGCTGGTGGTGCGACGGGGCCAGCCCTTCTGG
CTGACCCTGCACTTTGAGGGCCGCAACTACCAGGCCAGTGTAGACAGTCTCACCTTCAGT
GTCGTGACCGGCCCAGCCCCTAGCCAGGAGGCCGGGACCAAGGCCCGTTTTCCACTAAGA
GATGCTGTGGAGGAGGGTGACTGGACAGCCACCGTGGTGGACCAGCAAGACTGCACCCTC
TCGCTGCAGCTCACCACCCCGGCCAACGCCCCCATCGGCCTGTATCGCCTCAGCCTGGAG
GCCTCCACTGGCTACCAGGGATCCAGCTTTGTGCTGGGCCACTTCATTTTGCTCTTCAAC
GCCTGGTGCCCAGCGGATGCTGTGTACCTGGACTCGGAAGAGGAGCGGCAGGAGTATGTC
CTCACCCAGCAGGGCTTTATCTACCAGGGCTCGGCCAAGTTCATCAAGAACATACCTTGG
AATTTTGGGCAGTTTCAAGATGGGATCCTAGACATCTGCCTGATCCTTCTAGATGTCAAC
CCCAAGTTCCTGAAGAACGCCGGCCGTGACTGCTCCCGGCGCAGCAGCCCCGTCTACGTG
GGCCGGGTGGGTAGTGGCATGGTCAACTGCAACGATGACCAGGGTGTGCTGCTGGGACGC
TGGGACAACAACTACGGGGACGGCGTCAGCCCCATGTCCTGGATCGGCAGCGTGGACATC
CTGCGGCGCTGGAAGAACCACGGCTGCCAGCGCGTCAAGTATGGCCAGTGCTGGGTCTTC
GCCGCCGTGGCCTGCACAGTGCTGAGGTGCCTAGGCATCCCTACCCGCGTCGTGACCAAC
TACAACTCGGCCCATGACCAGAACAGCAACCTTCTCATCGAGTACTTCCGCAATGAGTTT
GGGGAGATCCAGGGTGACAAGAGCGAGATGATCTGGAACTTCCACTGCTGGGTGGAGTCG
TGGATGACCAGGCCGGACCTGCAGCCGGGGTACGAGGGCTGGCAGGCCCTGGACCCAACG
CCCCAGGAGAAGAGCGAAGGAACGTACTGCTGTGGCCCAGTTCCAGTTCGTGCCATCAAG
GAGGGCGACCTGAGCACCAAGTACGATGCGCCCTTTGTCTTTGCGGAGGTCAATGCCGAC
GTGGTAGACTGGATCCAGCAGGACGATGGGTCTGTGCACAAATCCATCAACCGTTCCCTG
ATCGTTGGGCTGAAGATCAGCACTAAGAGCGTGGGCCGAGACGAGCGGGAGGATATCACC
CACACCTACAAATACCCAGAGGGGTCCTCAGAGGAGAGGGAGGCCTTCACAAGGGCGAAC
CACCTGAACAAACTGGCCGAGAAGGAGGAGACAGGGATGGCCATGCGGATCCGTGTGGGC
CAGAGCATGAACATGGGCAGTGACTTTGACGTCTTTGCCCACATCACCAACAACACCGCT
GAGGAGTACGTCTGCCGCCTCCTGCTCTGTGCCCGCACCGTCAGCTACAATGGGATCTTG
GGGCCCGAGTGTGGCACCAAGTACCTGCTCAACCTAACCCTGGAGCCTTTCTCTGAGAAG
AGCGTTCCTCTTTGCATCCTCTATGAGAAATACCGTGACTGCCTTACGGAGTCCAACCTC
ATCAAGGTGCGGGCCCTCCTCGTGGAGCCAGTTATCAACAGCTACCTGCTGGCTGAGAGG
GACCTCTACCTGGAGAATCCAGAAATCAAGATCCGGATCCTTGGGGAGCCCAAGCAGAAA
CGCAAGCTGGTGGCTGAGGTGTCCCTGCAGAACCCGCTCCCTGTGGCCCTGGAAGGCTGC
ACCTTCACTGTGGAGGGGGCCGGCCTGACTGAGGAGCAGAAGACGGTGGAGATCCCAGAC
CCCGTGGAGGCAGGGGAGGAAGTTAAGGTGAGAATGGACCTCGTGCCGCTCCACATGGGC
CTCCACAAGCTGGTGGTGAACTTCGAGAGCGACAAGCTGAAGGCTGTGAAGGGCTTCCGG
AATGTCATCATTGGCCCCGCCTAA
Enzyme 9 GenBank Gene ID M55153 Link Image
Enzyme 9 GeneCard ID TGM2 Link Image
Enzyme 9 GenAtlas ID TGM2 Link Image
Enzyme 9 HGNC ID HGNC:11778 Link Image
Enzyme 9 Chromosome Location 20
Enzyme 9 Locus 20q12
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Gentile V, Saydak M, Chiocca EA, Akande O, Birckbichler PJ, Lee KN, Stein JP, Davies PJ: Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases. J Biol Chem. 1991 Jan 5;266(1):478-83. [PubMed Link Image]
  2. Fraij BM, Birckbichler PJ, Patterson MK Jr, Lee KN, Gonzales RA: A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue. J Biol Chem. 1992 Nov 5;267(31):22616-23. [PubMed Link Image]
  3. Fraij BM, Gonzales RA: A third human tissue transglutaminase homologue as a result of alternative gene transcripts. Biochim Biophys Acta. 1996 Apr 10;1306(1):63-74. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5943
Enzyme 10 Name Glutamine synthetase
Enzyme 10 Synonyms
  1. Glutamate--ammonia ligase
  2. GS
Enzyme 10 Gene Name GLUL
Enzyme 10 Protein Sequence >Glutamine synthetase 
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN
Enzyme 10 Number of Residues 373
Enzyme 10 Molecular Weight 42065
Enzyme 10 Theoretical pI 6.88
Enzyme 10 GO Classification
Function
  • acid-ammonia (or amide) ligase activity
  • acid-ammonia (or amide) ligase activity
  • ammonia ligase activity
  • catalytic activity
  • glutamate-ammonia ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glutamine biosynthesis
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
—
Enzyme 10 General Function Amino acid transport and metabolism
Enzyme 10 Specific Function ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + L-glutamate + ammonia = ADP + phosphate + L-glutamine
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 31833 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P15104 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name GLNA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1122 bp 
ATGACCACCTCAGCAAGTTCCCACTTAAATAAAGGCATCAAGCAGGTGTACATGTCCCTG
CCTCAGGGTGAGAAAGTCCAGGCCATGTATATCTGGATCGATGGTACTGGAGAAGGACTG
CGCTGCAAGACCCGGACCCTGGACAGTGAGCCCAAGTGTGTGGAAGAGTTGCCTGAGTGG
AATTTCGATGGCTCCAGTACTTTACAGTCTGAGGGTTCCAACAGTGACATGTATCTCGTG
CCTGCTGCCATGTTTCGGGACCCCTTCCGTAAGGACCCTAACAAGCTGGTGTTATGTGAA
GTTTTCAAGTACAATCGAAGGCCTGCAGAGACCAATTTGAGGCACACCTGTAAACGGATA
ATGGACATGGTGAGCAACCAGCACCCCTGGTTTGGCATGGAGCAGGAGTATACCCTCATG
GGGACAGATGGGCACCCCTTTGGTTGGCCTTCCAACGGCTTCCCAGGGCCCCAGGGTCCA
TATTACTGTGGTGTGGGAGCAGACAGAGCCTATGGCAGGGACATCGTGGAGGCCCATTAC
CGGGCCTGCTTGTATGCTGGAGTCAAGATTGCGGGGACTAATGCCGAGGTCATGCCTGCC
CAGTGGGAATTTCAGATTGGACCTTGTGAAGGAATCAGCATGGGAGATCATCTCTGGGTG
GCCCGTTTCATCTTGCATCGTGTGTGTGAAGACTTTGGAGTGATAGCAACCTTTGATCCT
AAGCCCATTCCTGGGAACTGGAATGGTGCAGGCTGCCATACCAACTTCAGCACCAAGGCC
ATGCGGGAGGAGAATGGTCTGAAGTACATCGAGGAGGCCATTGAGAAACTAAGCAAGCGG
CACCAGTACCACATCCGTGCCTATGATCCCAAGGGAGGCCTGGACAATGCCCGACGTCTA
ACTGGATTCCATGAAACCTCCAACATCAACGACTTTTCTGGTGGTGTAGCCAATCGTAGC
GCCAGCATACGCATTCCCCGGACTGTTGGCCAGGAGAAGAAGGGTTACTTTGAAGATCGT
CGCCCCTCTGCCAACTGCGACCCCTTTTCGGTGACAGAAGCCCTCATCCGCACGTGTCTT
CTCAATGAAACCGGCGATGAGCCCTTCCAGTACAAAAATTAA
Enzyme 10 GenBank Gene ID Y00387 Link Image
Enzyme 10 GeneCard ID GLUL Link Image
Enzyme 10 GenAtlas ID GLUL Link Image
Enzyme 10 HGNC ID HGNC:4341 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1q31
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Gibbs CS, Campbell KE, Wilson RH: Sequence of a human glutamine synthetase cDNA. Nucleic Acids Res. 1987 Aug 11;15(15):6293. [PubMed Link Image]
  2. Van den Hoff MJ, Geerts WJ, Das AT, Moorman AF, Lamers WH: cDNA sequence of the long mRNA for human glutamine synthase. Biochim Biophys Acta. 1991 Oct 8;1090(2):249-51. [PubMed Link Image]
  3. Christa L, Simon MT, Flinois JP, Gebhardt R, Brechot C, Lasserre C: Overexpression of glutamine synthetase in human primary liver cancer. Gastroenterology. 1994 May;106(5):1312-20. [PubMed Link Image]
  4. Boksha IS, Schonfeld HJ, Langen H, Muller F, Tereshkina EB, Burbaeva GSh: Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase. Biochemistry (Mosc). 2002 Sep;67(9):1012-20. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5945
Enzyme 11 Name Coagulation factor XIII A chain precursor
Enzyme 11 Synonyms
  1. Coagulation factor XIIIa
  2. Protein-glutamine gamma-glutamyltransferase A chain
  3. Transglutaminase A chain
Enzyme 11 Gene Name F13A1
Enzyme 11 Protein Sequence >Coagulation factor XIII A chain precursor 
MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDT
NKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPV
PIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETD
TYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCL
YVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDIL
LEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGN
VNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKH
GHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITD
TYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITF
RNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLL
EQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKET
LRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYG
ELDVQIQRRPSM
Enzyme 11 Number of Residues 732
Enzyme 11 Molecular Weight 83268
Enzyme 11 Theoretical pI 5.95
Enzyme 11 GO Classification
Function
—
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • peptide cross-linking
  • physiological process
  • protein modification
Component
—
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl- epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 182309 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P00488 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name F13A_HUMAN Link Image
Enzyme 11 PDB ID 1FIE Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2199 bp 
ATGTCAGAAACTTCCAGGACCGCCTTTGGAGGCAGAAGAGCAGTTCCACCCAATAACTCT
AATGCAGCGGAAGATGACCTGCCCACAGTGGAGCTTCAGGGCGTGGTGCCCCGGGGCGTC
AACCTGCAAGAGTTTCTTAATGTCACGAGCGTTCACCTGTTCAAGGAGAGATGGGACACT
AACAAGGTGGACCACCACACTGACAAGTATGAAAACAACAAGCTGATTGTCCGCAGAGGG
CAGTCTTTCTATGTGCAGATTGACTTCAGTCGTCCATATGACCCCAGAAGGGATCTCTTC
AGGGTGGAATACGTCATTGGTCGCTACCCACAGGAGAACAAGGGAACCTACATCCCAGTG
CCTATAGTCTCAGAGTTACAAAGTGGAAAGTGGGGGGCCAAGATTGTCATGAGAGAGGAC
AGGTCTGTGCGGCTGTCCATCCAGTCTTCCCCCAAATGTATTGTGGGGAAATTCCGCATG
TATGTTGCTGTCTGGACTCCCTATGGCGTACTTCGAACCAGTCGAAACCCAGAAACAGAC
ACGTACATTCTCTTCAATCCTTGGTGTGAAGATGATGCTGTGTATCTGGACAATGAGAAA
GAAAGAGAAGAGTATGTCCTGAATGACATCGGGGTAATTTTTTATGGAGAGGTCAATGAC
ATCAAGACCAGAAGCTGGAGCTATGGTCAGTTTGAAGATGGCATCCTGGACACTTGCCTG
TATGTGATGGACAGAGCACAAATGGACCTCTCTGGAAGAGGGAATCCCATCAAAGTCAGC
CGTGTGGGGTCTGCAATGGTGAATGCCAAAGATGACGAAGGTGTCCTCGTTGGATCCTGG
GACAATATCTATGCCTATGGCGTCCCCCCATCGGCCTGGACTGGAAGCGTTGACATTCTA
TTGGAATACCGGAGCTCTGAGAATCCAGTCCGGTATGGCCAATGCTGGGTTTTTGCTGGT
GTCTTTAACACATTTTTACGATGCCTTGGAATACCAGCAAGAATTGTTACCAATTATTTC
TCTGCCCATGATAATGATGCCAATTTGCAAATGGACATCTTCCTGGAAGAAGATGGGAAC
GTGAATTCCAAACTCACCAAGGATTCAGTGTGGAACTACCACTGCTGGAATGAAGCATGG
ATGACAAGGCCTGACCTTCCTGTTGGATTTGGAGGCTGGCAAGCTGTGGACAGCACCCCC
CAGGAAAATAGCGATGGCATGTATCGGTGTGGCCCCGCCTCGGTTCAAGCCATCAAGCAC
GGCCATGTCTGCTTCCAATTTGATGCACCTTTTGTTTTTGCAGAGGTCAACAGCGACCTC
ATTTACATTACAGCTAAGAAAGATGGCACTCATGTGGTGGAAAATGTGGATGCCACCCAC
ATTGGGAAATTAATTGTGACCAAACAAATTGGAGGAGATGGCATGATGGATATTACTGAT
ACTTACAAATTCCAAGAAGGTCAAGAAGAAGAGAGATTGGCCCTAGAAACTGCCCTGATG
TACGGAGCTAAAAAGCCCCTCAACACAGAAGGTGTCATGAAATCAAGGTCCAACGTTGAC
ATGGACTTTGAAGTGGAAAATGCTGTGCTGGGAAAAGACTTCAAGCTCTCCATCACCTTC
CGGAACAACAGCCACAACCGTTACACCATCACAGCTTATCTCTCAGCCAACATCACCTTC
TACACCGGGGTCCTGAAGGCAGAATTCAAGAAGGAGACGTTCGACGTGACGCTGGAGCCC
TTGTCCTTCAAGAAAGAGGCGGTGCTGATCCAAGCCGGCGAGTACATGGGTCAGCTGCTG
GAACAAGCGTCCCTGCACTTCTTTGTCACAGCTCGCATCAATGAGACCAGGGATGTTCTG
GCCAAGCAAAAGTCCACCGTGCTAACCATCCCTGAGATCATCATCAAGGTCCGTGGCACT
CAGGTAGTTGGTTCTGACATGACTGTGACAGTTCAGTTTACCAATCCTTTAAAAGAAACC
CTGCGAAATGTCTGGGTACACCTGGATGGTCCTGGAGTAACAAGACCAATGAAGAAGATG
TTCCGTGAAATCCGGCCCAACTCCACCGTGCAGTGGGAAGAAGTGTGCCGGCCCTGGGTC
TCTGGGCATCGGAAGCTGATAGCCAGCATGAGCAGTGACTCCCTGAGACATGTGTATGGC
GAGCTGGACGTGCAGATTCAAAGACGACCTTCCATGTGA
Enzyme 11 GenBank Gene ID M22001 Link Image
Enzyme 11 GeneCard ID F13A1 Link Image
Enzyme 11 GenAtlas ID F13A1 Link Image
Enzyme 11 HGNC ID HGNC:3531 Link Image
Enzyme 11 Chromosome Location 6
Enzyme 11 Locus 6p25.3-p24.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Ichinose A, Davie EW: Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proc Natl Acad Sci U S A. 1988 Aug;85(16):5829-33. [PubMed Link Image]
  2. Ichinose A, Hendrickson LE, Fujikawa K, Davie EW: Amino acid sequence of the a subunit of human factor XIII. Biochemistry. 1986 Nov 4;25(22):6900-6. [PubMed Link Image]
  3. Grundmann U, Amann E, Zettlmeissl G, Kupper HA: Characterization of cDNA coding for human factor XIIIa. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8024-8. [PubMed Link Image]
  4. Takahashi N, Takahashi Y, Putnam FW: Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8019-23. [PubMed Link Image]
  5. Takagi T, Doolittle RF: Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry. 1974 Feb 12;13(4):750-6. [PubMed Link Image]
  6. Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7296-300. [PubMed Link Image]
  7. Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC: Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res. 1995 Jun 1;78(5):389-97. [PubMed Link Image]
  8. Weiss MS, Metzner HJ, Hilgenfeld R: Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Lett. 1998 Feb 27;423(3):291-6. [PubMed Link Image]
  9. Fox BA, Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by x-ray crystallography. J Biol Chem. 1999 Feb 19;274(8):4917-23. [PubMed Link Image]
  10. Suzuki K, Iwata M, Ito S, Matsui K, Uchida A, Mizoi Y: Molecular basis for subtypic differences of the "a" subunit of coagulation factor XIII with description of the genesis of the subtypes. Hum Genet. 1994 Aug;94(2):129-35. [PubMed Link Image]
  11. Board P, Coggan M, Miloszewski K: Identification of a point mutation in factor XIII A subunit deficiency. Blood. 1992 Aug 15;80(4):937-41. [PubMed Link Image]
  12. Kangsadalampai S, Board PG: The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity. Blood. 1998 Oct 15;92(8):2766-70. [PubMed Link Image]
  13. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5948
Enzyme 12 Name Glutaminase liver isoform, mitochondrial precursor
Enzyme 12 Synonyms
  1. GLS
  2. L-glutamine amidohydrolase
  3. L-glutaminase
Enzyme 12 Gene Name GLS2
Enzyme 12 Protein Sequence >Glutaminase liver isoform, mitochondrial precursor 
MRSMKALQKALSRAGSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQD
HDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQ
ESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVA
AYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHK
FVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAG
NEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESG
SVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGA
ILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGA
EIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE
ACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLES
MV
Enzyme 12 Number of Residues 602
Enzyme 12 Molecular Weight 66324
Enzyme 12 Theoretical pI 7.32
Enzyme 12 GO Classification
Function
  • catalytic activity
  • glutaminase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 12 General Function Amino acid transport and metabolism
Enzyme 12 Specific Function Plays an important role in the regulation of glutamine catabolism
Enzyme 12 Pathways
Enzyme 12 Reactions
  • L-glutamine + H2O = L-glutamate + NH3
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 6650606 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9UI32 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name GLSL_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1809 bp 
ATGCGCTCCATGAAGGCTCTGCAGAAGGCCCTGAGCCGGGCTGGCAGTCACTGCGGGCGA
GGAGGCTGGGGTCACCCGAGCCGGAGCCCCCTCCTTGGCGGGGGCGTCCGGCACCACCTC
AGTGAGGCCGCGGCGCAGGGCAGAGAGACGCCACACAGCCACCAGCCGCAGCACCAGGAT
CATGATTCATCAGAAAGTGGCATGCTGTCCCGCCTGGGTGATTTGCTCTTTTACACTATT
GCTGAAGGACAGGAACGAACCCCTATCCACAAGTTCACCACTGCACTAAAGGCCACTGGA
CTGCAGACATCAGATCCTCGGCTCCGAGACTGCATGAGCGAGATGCACCGCGTGGTCCAA
GAGTCCAGTAGTGGTGGCCTCTTGGACCGAGATCTCTTCCGAAAGTGTGTGAGCAGCAGC
ATTGTGCTCCTGACCCAGGCATTCCGAAAGAAGTTTGTCATTCCTGATTTTGAGGAGTTC
ACGGGCCATGTGGATCGCATCTTTGAGGATGTCAAAGAGCTCACTGGAGGCAAAGTGGCA
GCCTACATCCCTCAGCTGGCCAAGTCAAACCCAGACCTGTGGGGTGTCTCCCTGTGCACT
GTGGATGGTCAACGGCACTCTGTGGGCCACACAAAGATCCCCTTCTGCCTGCAGTCCTGT
GTGAAGCCCCTCACCTATGCCATCTCCATAAGCACCCTAGGCACTGACTACGTGCACAAG
TTTGTGGGCAAAGAGCCAAGTGGCCTGCGCTACAACAAGCTCTCCCTCGATGAGGAAGGA
ATCCCCCATAACCCCATGGTCAATGCTGGTGCCATTGTTGTCAGCTCCCTGATCAAGATG
GACTGTAACAAAGCAGAGAAGTTTGATTTTGTGTTGCAGTATCTCAACAAAATGGCTGGG
AATGAATACATGGGTTTCAGCAATGCCACATTCCAGTCAGAGAAGGAAACAGGGGATCGG
AATTATGCCATCGGCTATTATCACGAGGAAAAGAAGTGCTTTCCTAAGGGGGTGGACATG
ATGGCTGCCCTTGATCTCTACTTCCAGCTGTGTTCTGTGGAGGTCACTTGTGAATCAGGC
AGTGTCATGGCAGCCACCCTCGCCAACGGTGGGATTTGCCCCATCACAGGCGAGAGTGTG
CTGAGTGCTGAAGCAGTGCGCAACACCCTCAGCCTCATGCATTCCTGCGGCATGTATGAC
TTCTCTGGCCAGTTTGCCTTCCACGTGGGCCTGCCAGCCAAGTCAGCTGTATCAGGAGCC
ATCCTCCTGGTGGTACCCAATGTCATGGGAATGATGTGCCTGTCACCCCCATTGGACAAG
CTGGGGAACAGCCATAGGGGGACCAGCTTCTGCCAGAAGTTGGTGTCTCTCTTCAATTTC
CACAACTATGACAACCTGAGGCACTGTGCTCGGAAGTTAGACCCACGGCGTGAAGGGGCA
GAAATTCGGAACAAGACTGTGGTCAACCTGTTATTTGCTGCCTATAGTGGCGATGTCTCA
GCTCTTCGAAGGTTTGCCTTGTCAGCCATGGATATGGAACAGAAAGACTATGACTCGCGC
ACAGCTCTGCATGTTGCTGCAGCTGAAGGACACATCGAAGTTGTTAAATTCCTGATCGAG
GCTTGCAAAGTGAATCCTTTTGCCAAGGACAGGTGGGGCAACATTCCCCTGGATGATGCT
GTGCAGTTCAACCATCTGGAGGTGGTCAAACTGCTTCAAGATTACCAGGACTCCTACACA
CTCTCTGAAACTCAGGCTGAGGCAGCAGCTGAGGCCCTGTCCAAAGAGAACTTAGAAAGC
ATGGTATGA
Enzyme 12 GenBank Gene ID AF110330 Link Image
Enzyme 12 GeneCard ID GLS2 Link Image
Enzyme 12 GenAtlas ID GLS2 Link Image
Enzyme 12 HGNC ID HGNC:29570 Link Image
Enzyme 12 Chromosome Location 12
Enzyme 12 Locus 12q13
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Gomez-Fabre PM, Aledo JC, Del Castillo-Olivares A, Alonso FJ, Nunez De Castro I, Campos JA, Marquez J: Molecular cloning, sequencing and expression studies of the human breast cancer cell glutaminase. Biochem J. 2000 Jan 15;345 Pt 2:365-75. [PubMed Link Image]
  2. Olalla L, Aledo JC, Bannenberg G, Marquez J: The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins. FEBS Lett. 2001 Jan 19;488(3):116-22. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5949
Enzyme 13 Name CTP synthase 1
Enzyme 13 Synonyms
  1. UTP--ammonia ligase 1
  2. CTP synthetase 1
Enzyme 13 Gene Name CTPS
Enzyme 13 Protein Sequence >CTP synthase 1 
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Enzyme 13 Number of Residues 591
Enzyme 13 Molecular Weight 66691
Enzyme 13 Theoretical pI 6.42
Enzyme 13 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
—
Enzyme 13 General Function Nucleotide transport and metabolism
Enzyme 13 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Enzyme 13 Pathways
Enzyme 13 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 30293 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P17812 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PYRG1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1776 bp 
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
Enzyme 13 GenBank Gene ID X52142 Link Image
Enzyme 13 GeneCard ID CTPS Link Image
Enzyme 13 GenAtlas ID CTPS Link Image
Enzyme 13 HGNC ID HGNC:2519 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1p34.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5952
Enzyme 14 Name Protein-glutamine gamma-glutamyltransferase 5
Enzyme 14 Synonyms
  1. Transglutaminase-5
  2. TGase 5
  3. Transglutaminase X
  4. TGase X
  5. TGX
  6. TG(X
Enzyme 14 Gene Name TGM5
Enzyme 14 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 5 
MAQGLEVALTDLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFRNRSFQPGLDNIIFV
VETGPLPDLALGTRAVFSLARHHSPSPWIAWLETNGATSTEVSLCAPPTAAVGRYLLKIH
IDSFQGSVTAYQLGEFILLFNPWCPEDAVYLDSEPQRQEYVMNDYGFIYQGSKNWIRPCP
WNYGQFEDKIIDICLKLLDKSLHFQTDPATDCALRGSPVYVSRVVCAMINSNDDNGVLNG
NWSENYTDGANPAEWTGSVAILKQWNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVIT
NFDSGHDTDGNLIIDEYYDNTGRILGNKKKDTIWNFHVWNECWMARKDLPPAYGGWQVLD
ATPQEMSNGVYCCGPASVRAIKEGEVDLNYDTPFVFSMVNADCMSWLVQGGKEQKLHQDT
SSVGNFISTKSIQSDERDDITENYKYEEGSLQERQVFLKALQKLKARSFHGSQRGAELQP
SRPTSLSQDSPRSLHTPSLRPSDVVQVSLKFKLLDPPNMGQDICFVLLALNMSSQFKDLK
VNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYSQYLSTDKLIRISALG
EEKSSPEKILVNKIITLSYPSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVLTVEGS
GLFKKQQKVFLGVLKPQHQASIILETVPFKSGQRQIQANMRSNKFKDIKGYRNVYVDFAL
Enzyme 14 Number of Residues 720
Enzyme 14 Molecular Weight 80778
Enzyme 14 Theoretical pI 6.39
Enzyme 14 GO Classification
Function
—
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • peptide cross-linking
  • physiological process
  • protein modification
Component
—
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 2895530 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O43548 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name TGM5_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2163 bp 
ATGGCCCAAGGGCTAGAAGTGGCCCTCACAGACCTCCAGAGCTCCAGAAATAATGTGCGG
CACCACACGGAGGAGATCACTGTGGACCACCTGCTTGTTCGCCGGGGCCAGGCCTTCAAC
CTCACCCTGTACTTCAGGAACCGGAGCTTCCAGCCAGGCCTGGACAACATCATCTTCGTG
GTTGAAACTGGACCGCTGTCAGACCTGGCCTTGGGGACTCGGGCTGTGTTCAGCCTGGCA
CGCCATCACAGCCCCAGCCCCTGGATTGCCTGGCTGGAGACCAATGGGGCCACCTCCACA
GAGGTGAGCTTGTGCGCTCCTCCCACGGCGGCCGTGGGTCGGTACCTCTTGAAAATCCAC
ATCGACTCCTTCCAGGGGTCTGTGACGGCCTACCAGCTAGGGGAGTTCATCCTGCTTTTC
AATCCCTGGTGCCCAGAGGATGCTGTCTACTTGGACAGTGAACCCCAGAGGCAGGAGTAT
GTCATGAATGATTATGGCTTCATCTACCAAGGCAGCAAGAACTGGATCCGCCCATGTCCC
TGGAACTATGGACAGTTTGAAGACAAAATCATAGACATCTGCCTGAAGCTGCTAGACAAG
AGCCTGCACTTCCAGACTGACCCAGCCACAGACTGTGCTCTGCGGGGAAGCCCCGTCTAC
GTCAGCAGAGTGGTGTGTGCCATGATCAACAGCAATGATGATAATGGGGTGCTCAATGGA
AACTGGAGTGAGAATTACACAGACGGCGCCAACCCTGCGGAGTGGACGGGCAGCGTGGCC
ATCCTGAAGCAGTGGAACGCCACAGGCTGCCAGCCCGTGCGCTACGGGCAATGCTGGGTC
TTTGCTGCCGTCATGTGCACAGTGATGAGGTGTCTGGGGATCCCTACCCGTGTGATCACC
AACTTCGACTCTGGCCACGATACAGATGGAAACCTGATCATAGATGAGTATTATGACAAC
ACAGGCAGGATTTTGGGGAATAAGAAGAAGGATACTATCTGGAACTTCCATGTCTGGAAT
GAGTGCTGGATGGCCCGGAAGGATCTGCCCCCTGCATATGGAGGCTGGCAGGTGCTGGAC
GCCACACCTCAGGAGATGAGCAACGGCGTCTACTGCTGTGGCCCTGCCTCTGTCAGAGCC
ATCAAAGAAGGAGAAGTGGACCTGAACTATGACACGCCCTTTGTGTTTTCGATGGTGAAT
GCTGACTGCATGTCCTGGCTCGTCCAGGGAGGGAAGGAGCAGAAGCTTCACCAGGACACG
AGTTCTGTTGGCAATTTTATCAGCACAAAGAGCATCCAGAGTGACGAGCGGGATGACATC
ACAGAGAACTACAAGTATGAAGAAGGATCCCTCCAGGAGAGGCAGGTGTTTCTGAAGGCT
CTGCAGAAGCTGAAGGCTAGAAGCTTCCATGGCTCCCAAAGAGGAGCAGAGTTGCAACCT
TCCAGGCCCACATCACTGAGCCAGGACAGCCCTCGGAGCCTGCATACACCTTCCCTTCGA
CCCAGTGATGTGGTGCAAGTCTCCCTGAAATTCAAGCTGCTCGACCCGCCCAACATGGGC
CAGGATATATGCTTTGTCCTGCTGGCCCTCAACATGTCCTCCCAGTTCAAGGACCTCAAA
GTGAACCTGAGTGCCCAGTCTCTGCTGCACGATGGCAGCCCCCTGTCCCCATTCTGGCAG
GACACAGCGTTCATCACACTCTCTCCTAAAGAAGCAAAGACCTACCCCTGCAAAATCTCC
TATTCCCAGTACAGCCAGTACCTGTCAACAGACAAGCTGATCCGCATCAGTGCCCTGGGT
GAAGAGAAAAGCAGTCCTGAGAAAATCCTGGTGAACAAGATCATCACCTTATCTTATCCA
AGCATCACGATTAATGTTCTAGGAGCAGCCGTTGTGAACCAGCCACTCTCCATACAGGTG
ATATTTTCAAACCCCCTCTCGGAGCAGGTTGAGGACTGTGTGCTGACTGTGGAAGGAAGT
GGCCTCTTCAAGAAACAGCAGAAAGTCTTCCTTGGAGTCCTCAAACCCCAACACCAAGCA
AGCATCATTCTGGAGACCGTCCCCTTCAAGAGTGGACAAAGGCAGATCCAAGCTAATATG
AGAAGCAACAAGTTTAAGGACATTAAGGGTTACAGGAATGTTTATGTAGACTTTGCATTA
TAA
Enzyme 14 GenBank Gene ID AF035960 Link Image
Enzyme 14 GeneCard ID TGM5 Link Image
Enzyme 14 GenAtlas ID TGM5 Link Image
Enzyme 14 HGNC ID HGNC:11781 Link Image
Enzyme 14 Chromosome Location 15
Enzyme 14 Locus 15q15.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF: Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers. J Biol Chem. 1998 Feb 6;273(6):3452-60. [PubMed Link Image]
  2. Grenard P, Bates MK, Aeschlimann D: Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z. J Biol Chem. 2001 Aug 31;276(35):33066-78. Epub 2001 Jun 4. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5953
Enzyme 15 Name Glutaminase kidney isoform, mitochondrial precursor
Enzyme 15 Synonyms
  1. GLS
  2. L-glutamine amidohydrolase
  3. K-glutaminase
Enzyme 15 Gene Name GLS
Enzyme 15 Protein Sequence >Glutaminase kidney isoform, mitochondrial precursor 
MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGG
GGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEG
KELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMD
MLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKK
QSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDL
GTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQ
FLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSI
EVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPA
KSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKL
DPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVE
VVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQT
VHKNLDGLL
Enzyme 15 Number of Residues 669
Enzyme 15 Molecular Weight 73462
Enzyme 15 Theoretical pI 7.82
Enzyme 15 GO Classification
Function
  • catalytic activity
  • glutaminase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 15 General Function Amino acid transport and metabolism
Enzyme 15 Specific Function Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine
Enzyme 15 Pathways
Enzyme 15 Reactions
  • L-glutamine + H2O = L-glutamate + NH3
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-23
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 5690372 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O94925 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name GLSK_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1797 bp 
ATGATGCGGCTGCGAGGCTCGGGGATGCTGCGGGACCTGCTCCTGCGGTCGCCCGCCGGC
GTGAGCGNGACTCTGCGGCGGGCACAGCCCTTGGTCACCCTGTGCCGGCGTCCCCGAGGC
GGGGGACGGCCGGCCGCGGGCCCGGCTGCCGCCGCGCGACTCCACCCGTGGTGGGGCGGG
GGCGGCTGGCCGGCGGAGCCCCTCGCGCGGGGCCTGTCCAGCTCTCCTTCGGAGATCTTG
CAGGAGCTGGGCAAGGGGAGCACGCATCCCCAGCCCGGGGTGTCGCCACCCGCTGCCCCG
GCGGCGCCCGGCCCCAAGGACGGCCCCGGGGAGACGGACGCGTTTGGCAACAGCGAGGGC
AAAGAGCTGGTGGCCTCAGGTGAAAACAAAATAAAACAGGGTCTGTTACCTAGCTTGGAA
GATTTGCTGTTCTATACAATTGCTGAAGGACAAGAGAAAATACCTGTTCATAAATTTATT
ACAGCACTCAAATCTACAGGATTGCGAACGTCTGATCCCAGGTTGAAAGAGTGTATGGAT
ATGTTAAGATTAACTCTTCAAACAACATCAGATGGTGTCATGCTAGACAAAGATCTTTTT
AAAAAATGTGTTCAGAGCAACATTGTTTTGTTGACACAAGCATTTAGAAGAAAGTTTGTG
ATTCCTGACTTTATGTCTTTTACCTCACACATTGATGAGTTATATGAAAGTGCTAAAAAG
CAGTCTGGAGGAAAGGTTGCAGATTATATTCCTCAACTGGCCAAATTCAGTCCCGATTTG
TGGGGTGTGTCTGTTTGTACAGCAGATGGACAGAGGCATTCTACTGGAGATACCAAAGTT
CCCTTCTGTCTTCAGTCCTGTGTAAAACCTTTGAAATATGCCATTGCTGTTAATGATCTT
GGAACTGAATATGTGCATCGATATGTTGGAAAAGAGCCGAGTGGACTAAGATTCAACAAA
CTATTTTTGAATGAAGATGATAAACCACATAATCCTATGGTAAATGCTGGAGCAATTGTT
GTGACTTCACTAATAAAGCAAGGAGTAAATAATGCTGAAAAATTTGACTATGTCATGCAG
TTTTTGAATAAGATGGCTGGTAATGAATATGTTGGATTCAGTAATGCAACGTTTCAGTCT
GAAAGAGAAAGTGGAGATCGAAATTTTGCAATAGGATATTACTTAAAAGAAAAGAAGTGT
TTTCCAGAAGGCACAGACATGGTTGGTATATTAGACTTCTACTTCCAGCTGTGCTCCATT
GAAGTGACTTGTGAATCAGCCAGTGTGATGGCTGCGACACTGGCTAATGGTGGTTTCTGC
CCAATTACTGGTGAAAGAGTACTGAGCCCTGAAGCAGTTCGAAATACATTGAGTTTGATG
CATTCCTGTGGCATGTATGACTTCTCAGGGCAGTTTGCTTTCCATGTTGGTCTTCCTGCA
AAATCTGGAGTTGCTGGGGGCATTCTTTTAGTTGTCCCCAATGTTATGGGTATGATGTGC
TGGTCTCCTCCTCTGGATAAGATGGGCAACAGTGTTAAGGGAATTCACTTTTGTCACGAT
CTTGTTTCTCTGTGTAATTTCCATAACTATGATAATTTGAGACACTTTGCAAAAAAACTT
GATCCTCGAAGAGAAGGTGGTGATCAAAGGCATTCCTTTGGACCATTGGACTATGAAAGT
CTCCAACAAGAACTTGCTTTAAAAGAGACAGTATGGAAAAAAGTGTCACCTGAGTCAAAT
GAGGACATCTCTACAACTGTAGTATATAGAATGGAAAGTCTGGGAGAGAAAAGCTAA
Enzyme 15 GenBank Gene ID AF158555 Link Image
Enzyme 15 GeneCard ID GLS Link Image
Enzyme 15 GenAtlas ID GLS Link Image
Enzyme 15 HGNC ID HGNC:4331 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q32-q34
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Elgadi KM, Meguid RA, Qian M, Souba WW, Abcouwer SF: Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing. Physiol Genomics. 1999 Aug 31;1(2):51-62. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
  3. Holcomb T, Taylor L, Trohkimoinen J, Curthoys NP: Isolation, characterization and expression of a human brain mitochondrial glutaminase cDNA. Brain Res Mol Brain Res. 2000 Mar 10;76(1):56-63. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5955
Enzyme 16 Name Protein-glutamine gamma-glutamyltransferase K
Enzyme 16 Synonyms
  1. Transglutaminase K
  2. TGase K
  3. TGK
  4. TG(K
  5. Transglutaminase-1
  6. Epidermal TGase
Enzyme 16 Gene Name TGM1
Enzyme 16 Protein Sequence >Protein-glutamine gamma-glutamyltransferase K 
MMDGPRSDVGRWGGNPLQPPTTPSPEPEPEPDGRSRRGGGRSFWARCCGCCSCRNAADDD
WGPEPSDSRGRGSSSGTRRPGSRGSDSRRPVSRGSGVNAAGDGTIREGMLVVNGVDLLSS
RSDQNRREHHTDEYEYDELIVRRGQPFHMLLLLSRTYESSDRITLELLIGNNPEVGKGTH
VIIPVGKGGSGGWKAQVVKASGQNLNLRVHTSPNAIIGKFQFTVRTQSDAGEFQLPFDPR
NEIYILFNPWCPEDIVYVDHEDWRQEYVLNESGRIYYGTEAQIGERTWNYGQFDHGVLDA
CLYILDRRGMPYGGRGDPVNVSRVISAMVNSLDDNGVLIGNWSGDYSRGTNPSAWVGSVE
ILLSYLRTGYSVPYGQCWVFAGVTTTVLRCLGLATRTVTNFNSAHDTDTSLTMDIYFDEN
MKPLEHLNHDSVWNFHVWNDCWMKRPDLPSGFDGWQVVDATPQETSSGIFCCGPCSVESI
KNGLVYMKYDTPFIFAEVNSDKVYWQRQDDGSFKIVYVEEKAIGTLIVTKAISSNMREDI
TYLYKHPEGSDAERKAVETAAAHGSKPNVYANRGSAEDVAMQVEAQDAVMGQDLMVSVML
INHSSSRRTVKLHLYLSVTFYTGVSGTIFKETKKEVELAPGASDRVTMPVAYKEYRPHLV
DQGAMLLNVSGHVKESGQVLAKQHTFRLRTPDLSLTLLGAAVVGQECEVQIVFKNPLPVT
LTNVVFRLEGSGLQRPKILNVGDIGGNETVTLRQSFVPVRPGPRQLIASLDSPQLSQVHG
VIQVDVAPAPGDGGFFSDAGGDSHLGETIPMASRGGA
Enzyme 16 Number of Residues 817
Enzyme 16 Molecular Weight 89788
Enzyme 16 Theoretical pI 5.92
Enzyme 16 GO Classification
Function
—
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • peptide cross-linking
  • physiological process
  • protein modification
Component
—
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross- linking epidermal proteins during formation of the stratum corneum
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 1256959 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P22735 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name TGM1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2454 bp 
ATGATGGATGGGCCACGTTCCGATGTGGGCCGTTGGGGTGGCAACCCCTTGCAGCCCCCT
ACCACGCCATCTCCAGAGCCAGAGCCAGAGCCAGACGGACGCTCTCGCAGAGGAGGAGGC
CGTTCCTTCTGGGCTCGCTGCTGTGGCTGCTGTTCATGCCGAAATGCGGCAGATGACGAC
TGGGGACCTGAACCCTCTGACTCCAGGGGTCGAGGGTCCAGCTCTGGCACTCGAAGACCT
GGCTCCCGGGGCTCAGACTCCCGCCGGCCTGTATCCCGGGGCAGCGGTGTCAATGCAGCT
GGAGATGGCACCATCCGAGAGGGCATGCTAGTAGTGAACGGTGTGGACTTGCTGAGCTCG
CGCTCGGACCAGAACCGCCGAGAGCACCACACAGACGAGTATGAGTACGACGAGCTGATA
GTGCGCCGCGGGCAGCCTTTCCATATGCTCCTCCTCCTGTCCCGGACCTATGAATCCTCT
GATCGCATCACCCTTGAGTTACTCATCGGAAACAACCCCGAGGTGGGCAAGGGCACGCAC
GTGATCATCCCAGTGGGCAAGGGGGGCAGTGGAGGCTGGAAAGCCCAGGTGGTCAAGGCC
AGTGGGCAGAATCTGAACCTGCGGGTCCACACTTCCCCCAACGCCATCATCGGCAAGTTT
CAGTTCACAGTCCGCACACAATCAGACGCTGGGGAGTTCCAGTTGCCCTTTGACCCCCGC
AATGAGATCTACATCCTCTTCAACCCCTGGTGCCCAGAGGACATTGTGTACGTGGACCAT
GAGGATTGGCGGCAGGAGTATGTTCTTAATGAGTCTGGGAGAATTTACTACGGGACCGAA
GCACAGATTGGTGAGCGGACCTGGAACTACGGCCAGTTTGACCACGGGGTGCTGGATGCC
TGCTTATACATCCTGGACCGGCGGGGGATGCCATATGGAGGCCGTGGAGACCCAGTCAAT
GTCTCCCGGGTCATCTCTGCCATGGTGAACTCCCTGGATGACAATGGAGTCCTGATTGGG
AACTGGTCTGGTGATTACTCCCGAGGCACCAACCCATCAGCGTGGGTGGGCAGCGTGGAG
ATCCTGCTTAGCTACCTACGCACGGGATATTCCGTCCCCTATGGCCAGTGCTGGGTCTTT
GCTGGCGTGACCACCACAGTGCTGCGCTGCCTGGGTCTGGCCACCCGTACTGTCACCAAC
TTCAACTCCGCCCACGACACAGACACATCCCTTACCATGGACATCTACTTCGACGAGAAC
ATGAAGCCCCTGGAGCACCTGAACCATGATTCTGTCTGGAACTTCCATGTGTGGAACGAC
TGCTGGATGAAGAGGCCGGATCTGCCCTCGGGCTTTGATGGGTGGCAGGTGGTGGATGCC
ACACCCCAAGAGACTAGCAGTGGCATCTTCTGCTGCGGCCCCTGCTCTGTGGAGTCCATC
AAGAATGGCCTGGTCTACATGAAGTACGACACGCCTTTCATTTTTGCTGAGGTGAATAGT
GACAAGGTGTACTGGCAGCGGCAGGATGATGGCAGCTTCAAGATTGTTTATGTGGAGGAG
AAGGCCATCGGCACACTCATTGTCACAAAGGCCATCAGCTCCAACATGCGGGAGGACATC
ACCTACCTCTATAAGCACCCAGAAGGCTCAGACGCAGAGCGGAAGGCAGTAGAGACAGCA
GCAGCCCACGGCAGCAAACCCAATGTGTATGCCAACCGGGGCTCAGCGGAGGATGTGGCC
ATGCAGGTGGAGGCACAGGACGCGGTGATGGGGCAGGATCTGATGGTCTCTGTGATGCTG
ATCAATCACAGCAGCAGCCGCCGCACAGTGAAACTGCACCTCTACCTCTCAGTCACTTTC
TATACTGGTGTCAGTGGTACCATCTTCAAGGAGACCAAGAAGGAAGTGGAGCTGGCACCA
GGGGCCTCGGACCGTGTGACCATGCCAGTGGCCTACAAGGAATACCGGCCCCATCTTGTG
GACCAGGGGGCCATGCTGCTCAATGTCTCAGGCCACGTCAAGGAGAGCGGGCAGGTGCTG
GCCAAGCAGCACACCTTCCGTCTGCGCACCCCAGACCTCTCCCTCACGTTACTGGGAGCA
GCAGTGGTTGGCCAGGAGTGTGAAGTACAGATTGTCTTCAAGAACCCCCTTCCCGTCACC
CTCACCAATGTCGTCTTCCGGCTCGAAGGCTCTGGGTTACAGAGGCCCAAGATCCTCAAC
GTTGGGGACATTGGAGGCAATGAAACAGTGACACTGCGCCAGTCGTTTGTGCCTGTGCGA
CCAGGCCCCCGCCAGCTCATTGCCAGCTTGGACAGCCCACAGCTCTCCCAGGTGCACGGT
GTCATCCAGGTGGATGTGGCCCCAGCCCCTGGGGATGGGGGCTTCTTCTCAGACGCTGGA
GGTGACAGTCACTTAGGAGAGACCATCCCTATGGCATCTCGAGGTGGAGCTTAG
Enzyme 16 GenBank Gene ID M98447 Link Image
Enzyme 16 GeneCard ID TGM1 Link Image
Enzyme 16 GenAtlas ID TGM1 Link Image
Enzyme 16 HGNC ID HGNC:11777 Link Image
Enzyme 16 Chromosome Location 14
Enzyme 16 Locus 14q11.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Phillips MA, Stewart BE, Rice RH: Genomic structure of keratinocyte transglutaminase. Recruitment of new exon for modified function. J Biol Chem. 1992 Feb 5;267(4):2282-6. [PubMed Link Image]
  2. Kim HC, Idler WW, Kim IG, Han JH, Chung SI, Steinert PM: The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones. J Biol Chem. 1991 Jan 5;266(1):536-9. [PubMed Link Image]
  3. Phillips MA, Stewart BE, Qin Q, Chakravarty R, Floyd EE, Jetten AM, Rice RH: Primary structure of keratinocyte transglutaminase. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9333-7. [PubMed Link Image]
  4. Yamanishi K, Liew FM, Konishi K, Yasuno H, Doi H, Hirano J, Fukushima S: Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture. Biochem Biophys Res Commun. 1991 Mar 29;175(3):906-13. [PubMed Link Image]
  5. Polakowska RR, Eickbush T, Falciano V, Razvi F, Goldsmith LA: Organization and evolution of the human epidermal keratinocyte transglutaminase I gene. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4476-80. [PubMed Link Image]
  6. Yamanishi K, Inazawa J, Liew FM, Nonomura K, Ariyama T, Yasuno H, Abe T, Doi H, Hirano J, Fukushima S: Structure of the gene for human transglutaminase 1. J Biol Chem. 1992 Sep 5;267(25):17858-63. [PubMed Link Image]
  7. Schroeder WT, Thacher SM, Stewart-Galetka S, Annarella M, Chema D, Siciliano MJ, Davies PJ, Tang HY, Sowa BA, Duvic M: Type I keratinocyte transglutaminase: expression in human skin and psoriasis. J Invest Dermatol. 1992 Jul;99(1):27-34. [PubMed Link Image]
  8. Huber M, Rettler I, Bernasconi K, Frenk E, Lavrijsen SP, Ponec M, Bon A, Lautenschlager S, Schorderet DF, Hohl D: Mutations of keratinocyte transglutaminase in lamellar ichthyosis. Science. 1995 Jan 27;267(5197):525-8. [PubMed Link Image]
  9. Russell LJ, DiGiovanna JJ, Rogers GR, Steinert PM, Hashem N, Compton JG, Bale SJ: Mutations in the gene for transglutaminase 1 in autosomal recessive lamellar ichthyosis. Nat Genet. 1995 Mar;9(3):279-83. [PubMed Link Image]
  10. Laiho E, Ignatius J, Mikkola H, Yee VC, Teller DC, Niemi KM, Saarialho-Kere U, Kere J, Palotie A: Transglutaminase 1 mutations in autosomal recessive congenital ichthyosis: private and recurrent mutations in an isolated population. Am J Hum Genet. 1997 Sep;61(3):529-38. [PubMed Link Image]
  11. Akiyama M, Takizawa Y, Kokaji T, Shimizu H: Novel mutations of TGM1 in a child with congenital ichthyosiform erythroderma. Br J Dermatol. 2001 Feb;144(2):401-7. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5964
Enzyme 17 Name Protein-glutamine gamma-glutamyltransferase 6
Enzyme 17 Synonyms
  1. Transglutaminase-3-like
  2. TGase-3-like
  3. Transglutaminase Y
Enzyme 17 Gene Name TGM6
Enzyme 17 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 6 
MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMET
GPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSS
HRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYG
QFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQG
KYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNS
AHDTDQNLSVDKYVDSFGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYNGWQVLDATPQ
EESEGVFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDESRERVYSNTKKI
GRCISTKAVGSDSRVDITDLYKYPEGSRKERQVYSKAVNRLFGVEASGRRIWIRRAGGRC
LWRDDLLEPATKPSIAGKFKVLEPPMLGHDLRLALCLANLTSRAQRVRVNLSGATILYTR
KPVAEILHESHAVRLGPQEEKRIPITISYSKYKEDLTEDKKILLAAMCLVTKGEKLLVEK
DITLEDFITIKVLGPAMVGVAVTVEVTVVNPLIERVKDCALMVEGSGLLQEQLSIDVPTL
EPQERASVQFDITPSKSGPRQLQVDLVSPHFPDIKGFVIVHVATAK
Enzyme 17 Number of Residues 706
Enzyme 17 Molecular Weight 79313
Enzyme 17 Theoretical pI 7.26
Enzyme 17 GO Classification
Function
—
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • peptide cross-linking
  • physiological process
  • protein modification
Component
—
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 33331030 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O95932 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name TGM3L_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2121 bp 
ATGGCAGGGATCAGAGTCACCAAGGTGGACTGGCAGCGGTCGAGGAATGGCGCTGCCCAC
CACACCCAGGAGTACCCCTGCCCTGAGCTGGTGGTTCGCAGGGGCCAGTCGTTCAGCCTC
ACGCTGGAGCTGAGCAGAGCCCTGGACTGTGAGGAGATCCTCATCTTCACGGTGGAGACA
GGACCCCGGGCTTCTGAGGCCCTCCACACCAAAGCTGTGTTCCAGACATCGGAGCTGGAG
CGGGGTGAGGGCTGGACAGCAGCAAGGGAGGCTCAGATGGAGAAAACTCTGACCGTCAGT
CTCGCCAGCCCTCCCAGTGCTGTCATTGGCCGCTACCTGCTGAGCATCAGGCTTTCCTCT
CACCGCAAACACAGCAACCGGAGGCTGGGCGAGTTTGTTCTCCTTTTCAACCCATGGTGT
GCAGAGGACGATGTGTTTCTGGCCTCAGAGGAGGAGAGACAGGAGTACGTGCTCAGCGAC
AGCGGCATCATCTTCCGAGGCGTGGAGAAGCACATACGAGCCCAGGGCTGGAACTACGGG
CAGTTTGAGGAGGACATCCTGAACATCTGCCTCTCCATCCTGGATCGAAGCCCCGGTCAC
CAAAACAACCCAGCCACCGACGTGTCCTGCCGCCACAACCCCATCTACGTCACCAGGGTC
ATCAGTGCCATGGTGAACAGCAACAACGACCGAGGTGTGGTGCAAGGACAGTGGCAGGGC
AAGTACGGCGGCGGCACCAGCCCGCTGCACTGGCGCGGCAGCGTGGCCATTCTGCAGAAG
TGGCTCAAGGGCAGGTACAAGCCAGTCAAGTACGGCCAGTGCTGGGTCTTCGCCGGAGTC
CTGTGCACAGTCCTCAGGTGCTTGGGGATAGCCACACGGGTCGTGTCCAACTTCAACTCA
GCCCACGACACAGACCAGAACCTGAGTGTGGACAAATACGTGGACTCCTTCGGGCGGACC
CTGGAGGACCTGACAGAAGACAGCATGTGGAATTTCCATGTCTGGAATGAGAGCTGGTTT
GCCCGGCAGGACCTAGGCCCCTCTTACAATGGCTGGCAGGTTCTGGATGCCACCCCCCAG
GAGGAGAGTGAAGGTGTGTTCCGGTGCGGCCCAGCCTCAGTCACCGCCATCCGCGAGGGT
GATGTGCACCTGGCTCACGATGGCCCCTTCGTGTTTGCGGAGGTCAACGCCGACTACATC
ACCTGGCTGTGGCACGAGGATGAGAGCCGGGAGCGTGTATACTCAAACACGAAGAAGATT
GGGAGATGCATCAGCACCAAGGCGGTGGGCAGTGACTCCCGCGTGGACATCACTGACCTC
TACAAGTATCCGGAAGGGTCCCGGAAAGAGAGGCAGGTGTACAGCAAGGCGGTGAACAGG
CTGTTCGGCGTGGAAGCCTCTGGAAGGAGAATCTGGATCCGCAGGGCTGGGGGTCGCTGT
CTCTGGCGTGACGACCTCCTGGAGCCTGCCACCAAGCCCAGCATCGCTGGCAAGTTCAAG
GTGCTAGAGCCTCCCATGCTGGGCCACGACCTGAGACTGGCCCTGTGCTTGGCCAACCTC
ACCTCCCGGGCCCAGCGGGTGAGGGTCAACCTGAGCGGTGCCACCATCCTCTATACCCGC
AAGCCAGTGGCAGAGATCCTGCATGAATCCCACGCCGTGAGGCTGGGGCCGCAAGAAGAG
AAGAGAATCCCAATTACAATATCTTACTCTAAGTATAAAGAAGACCTGACAGAGGACAAG
AAGATCCTGTTGGCTGCCATGTGCCTTGTCACCAAAGGAGAGAAGCTTCTGGTGGAGAAG
GACATTACTCTAGAGGACTTCATCACCATCAAGGTTCTGGGCCCAGCCATGGTGGGAGTG
GCAGTTACAGTGGAAGTGACAGTAGTCAACCCCCTCATAGAGAGAGTGAAGGACTGTGCG
CTGATGGTGGAGGGCAGCGGCCTTCTCCAGGAACAGCTCAGCATCGACGTGCCTACCCTG
GAGCCTCAGGAGAGGGCCTCAGTCCAGTTTGACATCACCCCCTCCAAAAGTGGCCCAAGG
CAGCTGCAGGTGGACCTTGTAAGCCCTCACTTCCCGGACATCAAGGGCTTTGTGATCGTC
CATGTGGCCACTGCCAAGTGA
Enzyme 17 GenBank Gene ID AF540969 Link Image
Enzyme 17 GeneCard ID TGM6 Link Image
Enzyme 17 GenAtlas ID TGM6 Link Image
Enzyme 17 HGNC ID HGNC:16255 Link Image
Enzyme 17 Chromosome Location 20
Enzyme 17 Locus 20p13
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6134
Enzyme 18 Name Phosphoribosylformylglycinamidine synthase
Enzyme 18 Synonyms
  1. FGAM synthase
  2. FGAMS
  3. Formylglycinamide ribotide amidotransferase
  4. FGARAT
  5. Formylglycinamide ribotide synthetase
Enzyme 18 Gene Name PFAS
Enzyme 18 Protein Sequence >Phosphoribosylformylglycinamidine synthase 
MSPVLHFYVRPSGHEGAASGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKL
MWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVE
TTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEG
RLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLH
VDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQG
LRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGY
NLPWEDLSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREW
IKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLD
FGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTS
RFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVL
VDDRECPVRRNGQGDAPPTPPPTPVDLELEWVLGKMPRKEFFLQRKPPMLQPLALPPGLS
VHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIG
AATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAA
LADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTP
DLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLK
DRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPD
LAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDR
LQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMA
DAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAG
AELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLRHNLSG
RYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWA
DDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTS
PWLQLSINARNWTLEGSC
Enzyme 18 Number of Residues 1338
Enzyme 18 Molecular Weight 144666
Enzyme 18 Theoretical pI 5.55
Enzyme 18 GO Classification
Function
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • phosphoribosylformylglycinamidine synthase activity
Process
  • 'de novo' IMP biosynthesis
  • IMP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 18 General Function Nucleotide transport and metabolism
Enzyme 18 Specific Function ATP + 2-N-formyl-1-N-(5-phospho-D- ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- (formamido)-1-N-(5-phospho-D-ribosyl)acetamidine + L-glutamate
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 2224663 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O15067 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PUR4_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >4117 bp 
GGCCGCGAGTGCATCTTCCACGAACCTAATTCATCTCTCCAGCAAAGGACACATCTCTCC
AGCAAAGGACACCTCTCTCCAGCAAAGGACACCTGCAGAGATGTCCCCAGTCCTTCACTT
CTATGTTCGTCCCTCTGGCCATGAGGGGGCAGCCTCTGGACACACTCGGAGGAAACTGCA
AGGGAAACTGCCAGAGCTGCAGGGCGTCGAGACTGAACTGTGCTACAACGTGAACTGGAC
AGCTGAGGCCCTCCCCAGTGCTGAGGAGACAAAGAAGCTGATGTGGCTGTTTGGTTGCCC
CTTACTGCTGGATGATGTTGCTCGGGAGTCCTGGCTCCTTCCTGGCTCCAATGACCTGCT
GCTGGAGGTCGGGCCCAGGCTGAACTTCTCCACCCCAACATCCACCAACATCGTGTCAGT
GTGCCGCGCCACTGGGCTGGGGCCTGTGGATCGTGTGGAGACCACCCGGCGCTACCGGCT
CTCGTTTGCCCACCCCCCGTCAGCTGAGGTGGAAGCCATTGCTCTGGCTACCCTGCACGA
CCGGATGACAGAGCAGCACTTCCCCCATCCCATCCAGAGTTTCTCCCCTGAGAGCATGCC
GGAACCCCTCAATGGCCCTATCAATATACTGGGTGAGGGCCGGCTTGCGCTGGAGAAGGC
CAACCAGGAGCTTGGTCTGGCTTTAGACTCTTGGGACCTAGACTTCTACACCAAGCGCTT
CCAGGAGCTACAGCGGAACCCGAGCACTGTGGAGGCCTTTGACTTGGCGCAGTCCAATAG
CGAGCACAGCCGACACTGGTTCTTCAAGGGCCAGCTCCACGTGGATGGGCAGAAGCTGGT
GCACTCACTGTTTGAGTCCATCATGAGCACCCAGGAATCCTCGAACCCCAACAACGTCCT
CAAATTCTGTGATAACAGCAGTGCAATCCAGGGAAAGGAAGTCCGATTCCTACGGCCTGA
GGACCCCACACGGCCAAGCCGCTTCCAGCAACAGCAAGGGCTGAGACATGTTGTCTTCAC
AGCAGAGACTCACAACTTTCCCACAGGAGTATGCCCCTTTAGTGGTGCAACCACTGGCAC
AGGGGGCCGGATTCGAGATGTCCAGTGCACAGGCCGCGGGGCCCACGTGGTGGCTGGCAC
TGCCGGCTATTGCTTTGGAAATCTGCATATTCCAGGTTACAATCTGCCCTGGGAGGATCT
AAGCTTCCAGTATCCTGGGAATTTTGCCCGGCCCCTGGAGGTTGCCATTGAAGCCAGTAA
TGGAGCTTCTGACTATGGCAACAAGTTTGGGGAACCAGTGCTGGCTGGCTTCGCCCGCTC
CTTGGGCCTCCAGCTCCCAGACGGCCAGCGGCGTGAGTGGATCAAGCCCATCATGTTTAG
TGGGGGCATTGGGTCCATGGAAGCTGACCACATAAGCAAGGAGGCCCCAGAGCCAGGCAT
GGAAGTTGTAAAGGTTGGAGGTCCCGTCTACAGGATTGGAGTTGGAGGTGGAGCTGCTTC
ATCTGTGCAGGTGCAGGGAGATAACACCAGTGACCTGGACTTTGGGGCTGTGCAGCGAGG
AGACCCGGAGATGGAACAGAAGATGAACCGTGTGATCAGGGCTTGTGTGGAGGCCCCCAA
GGGAAACCCCATCTGCAGCCTTCATGATCAGGGCGCTGGTGGCAATGGCAATGTCCTAAA
AGAGCTGAGTGACCCAGCTGGAGCCATCATTTACACCAGCCGCTTCCAGCTTGGGGACCC
AACCCTGAATGCCCTGGAAATCTGGGGGGCTGAGTACCAGGAATCAAATGCTCTTCTGCT
GAGGTCCCCCAACCGGGACTTCCTGACTCATGTCAGTGCCCGTGAACGTTGCCCGGCTTG
CTTCGTGGGCACCATCACTGGAGACCGGAGAATAGTGCTGGTGGACGATCGGGAGTGTCC
TGTCAGAAGAAATGGCCAGGGGGATGCCCCCCCGACACCCCCGCCAACCCCTGTGGACCT
GGAGCTCGAATGGGTGCTGGGCAAGATGCCTCGGAAGGAGTTCTTCCTGCAGAGGAAGCC
CCCCATGCTGCAGCCTCTGGCCTTGCCCCCAGGGCTGAGCGTGCACCAGGCTCTGGAGAG
GGTTCTGAGGCTGCCCGCCGTGGCCAGCAAGCGCTACCTCACCAATAAGGTGGACCGCTC
CGTGGGAGGCCTGGTGGCCCAGCAGCAGTGCGTGGGGCCCCTGCAAACTCCTCTGGCAGA
TGTAGCGGTTGTGGCACTGAGCCATGAGGAGCTCATAGGGGCTGCCACAGCCTTGGGAGA
ACAGCCAGTCAAGAGCCTGCTGGACCCAAAAGTCGCCGCCCGGCTGGCCGTGGCCGAAGC
CCTCACCAACCTGGTGTTTGCTCTGGTCACTGACCTCCGGGATGTGAAGTGTAGCGGGAA
CTGGATGTGGGCAGCCAAGCTCCCAGGGGAGGGCGCAGCTTTGGCGGATGCCTGTGAGGC
TATGGTGGCAGTGATGGCAGCCCTGGGTGTGGCAGTGGATGGTGGCAAGGACTCCCTCAG
CATGGCTGCTCGGGTTGGCACTGAGACCGTGCGGGCTCCTGGGTCACTGGTCATCTCAGC
CTATGCCGTCTGCCCAGACATCACAGCCACTGTGACCCCAGACCTCAAGCATCCTGAAGG
GAGAGGCCATCTGCTCTATGTGGCTCTGAGCCCTGGGCAGCACCGGCTCGGGGGCACAGC
TCTGGCCCAGTGCTTCTCCCAGCTTGGGGAACACCCTCCAGACCTGGACCTTCCTGAGAA
CTTGGTGCGGGCCTTCAGCATCACTCAGGGGCTGCTGAAAGACCGCCTCCTCTGCTCAGG
CCACGATGTCAGTGACGGAGGCCTCGTCACATGCCTGCTGGAGATGGCCTTTGCTGGAAA
TTGCGGGCTACAGGTGGATGTGCCTGTCCCCAGGGTTGATGTCCTGTCTGTGCTGTTCGC
TGAGGAGCCAGGCCTCGTGCTGGAGGTGCAGGAGCCAGACCTGGCCCAGGTGCTGAAGCG
TTACCGGGATGCTGGCCTCCATTGCCTGGAGCTGGGCCACACAGGCGAGGCCGGGCCCCA
CGCCATGGTCCGGGTGTCAGTGAACGGGGCTGTGGTTCTGGAGGAGCCTGTTGGGGAGCT
GCGAGCCCTCTGGGAGGAGACGAGTTTCCAGCTGGACCGGCTACAGGCAGAGCCTCGCTG
TGTGGCAGAGGAGGAACGGGGCCTGAGGGAGCGGATGGGGCCCAGCTATTGCCTGCCCCC
CACCTTTCCCAAAGCCTCCGTGCCCCGTGAGCCTGGTGGTCCCAGCCCCCGAGTCGCCAT
CTTGCGAGAGGAGGGCAGTAATGGAGACCGGGAGATGGCCGATGCCTTCCACTTAGCTGG
GTTTGAGGTATGGGACGTGACCATGCAGGACCTCTGCTCTGGGGCAATTGGGCTGGACAC
TTTCCGTGGCGTGGCCTTCGTGGGCGGCTTCAGCTATGCAGATGTCCTGGGCTCTGCCAA
AGGGTGGGCAGCTGCTGTGACCTTTCATCCCAGGGCTGGGGCTGAGCTGAGGCGCTTCCG
GAAGCGGCCAGACACCTTCAGCCTGGGCGTGTGTAATGGCTGTCAACTGCTGGCTCTGCT
CGGCTGGGTGGGAGGCGACCCCAATGAGGATGCTGCAGAGATGGGCCCTGACTCCCAGCC
AGCCCGGCCAGGCCTTCTGCTACGCCACAACCTGTCTGGGCGCTACGAGTCTCGCTGGGC
CAGCGTGCGTGTGGGGCCTGGGCCAGCCCTGATGCTGCGAGGGATGGAGGGCGCCGTGCT
GCCCGTGTGGAGTGCGCACGGGGAAGGTTACGTAGCATTTTCTTCTCCGGAACTCCAAGC
TCAGATTGAGGCCAGGGGCTTGGCTCCACTGCACTGGGCTGATGATGACGGGAACCCCAC
AGAGCAGTACCCTCTGAATCCCAATGGGTCCCCAGGGGGCGTGGCTGGCATCTGCTCCTG
TGATGGCCGCCACCTGGCTGTCATGCCTCACCCTGAGCGGGCCGTTAGGCCTTGGCAGTG
GGCATGGCGACCCCCTCCATTTGATACTCTGACCACCTCCCCCTGGCTCCAGCTCTCTAT
CAATGCCCGAAACTGGACCCTGGAAGGGAGCTGCTGA
Enzyme 18 GenBank Gene ID AB002359 Link Image
Enzyme 18 GeneCard ID PFAS Link Image
Enzyme 18 GenAtlas ID PFAS Link Image
Enzyme 18 HGNC ID HGNC:8863 Link Image
Enzyme 18 Chromosome Location 17
Enzyme 18 Locus 17p13.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Patterson D, Bleskan J, Gardiner K, Bowersox J: Human phosphoribosylformylglycineamide amidotransferase (FGARAT): regional mapping, complete coding sequence, isolation of a functional genomic clone, and DNA sequence analysis. Gene. 1999 Nov 1;239(2):381-91. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 7366
Enzyme 19 Name Probable glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial precursor
Enzyme 19 Synonyms
  1. Glu-ADT subunit B
  2. Cytochrome oxidase assembly factor PET112 homolog
Enzyme 19 Gene Name PET112L
Enzyme 19 Protein Sequence >Probable glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial precursor 
MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGE
HKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAV
MTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIP
KTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQ
LILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQI
NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADP
QQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPK
KVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREG
KTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQS
RADPVMIKEILEKKLSL
Enzyme 19 Number of Residues 557
Enzyme 19 Molecular Weight 61865
Enzyme 19 Theoretical pI 8.86
Enzyme 19 GO Classification
Function
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • glutamyl-tRNA(Gln) amidotransferase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein biosynthesis
Component
—
Enzyme 19 General Function Translation, ribosomal structure and biogenesis
Enzyme 19 Specific Function Furnishes a means for formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu- tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho- Glu-tRNA(Gln) (Potential)
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-18
Enzyme 19 Transmembrane Regions Not Available
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 3599964 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O75879 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name GATB_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1674 bp 
ATGGCGGCGCCCATGCTGCGCTGGGGCTGCCGTGGAAGACGTTGGGCTTTCGCCCGGGTT
GACGGTGGTTCTTGCCACCGAAGAGGGGCTCCGACTGGGTCCACATCCAACCAGATTAGG
GGAGAGAGCTCAGTGGCTCAGCAGCCCCTCCACACGGCCCAGAAGACGAGGAAAGGTGAA
CACAAATGGGCTGCTGTGGTAGGTTTGGAAATTCATGCCCAGATTTCCTCCAACTCTAAA
CTCTTCTCTGGATCTCAAGTTCGCTTTTCAGCACCTCCAAATTCTTTGGTTTCTTTTTTT
GATGCATCTCTACCTGGAACTTTGCCGGTTCTCAACAGGAGGTGTGTAGAAGCGGCGGTG
ATGACAGGCCTGGCTCTGAACTGCCACATAAACAAGAAGTCCTTGTTTGACAGGAAGCAC
TACTTCTATGCAGACCTCCCTGCAGGCTACCAAATTACCCAGCAGAGGCTCCCAATTGCT
GTGAATGGGAGCTTGATATATGGCGTCTGTGCAGGGAAGAAGCAGAGTCAGGTGATCCCC
AAGACGGTGAGGATCAAGCAGATCCAGTTGGAGCAAGACAGTGGCAAAAGCCTCCACGAC
AACCTGAGGTCTCAGACGCTCATTGATTTGAACAGGGCAGGAGTGGGCCTTCTGGAGGTG
GTCCTGGAGCCCGACATGTCCTGTGGAGAAGAGGCGGCAACAGCTGTCAGGGAGCTGCAG
CTGATCCTTCAAGCCCTGGGGACCAGCCAGGCGAACATGGCAGAGGGCCAGTTGAGAGTG
GATGCCAATATATCCGTGCATCACCCTGGGGAGCCTTTGGGCGTTCGAACGGAAGTGAAG
AATCTCAACAGCATCAGGTTCCTGGCCAAAGCCATAGACTATGAAATTCAGAGGCAAATC
AATGAACTTGAGAATGGAGGTGAAATTCTGAACGAAACACGCTCATTTCATCACAAGCTG
GGGTGCACCATGTCAATGAGAGACAAAGAAGGAAAACAGGACTACAGGTTCATGCCAGAA
CCCAACCTGCCTCCCCTGGTGCTCTACGACGCCACATCTCTGCCCGCAGGTGCAGACCCA
CAGCAAGTGATCAATATTGACCAGATTCGGGAGACACTCCCGGAGCTCCCCAGTGTGACC
CGAGAGAAGCTTGTCCAACAGTATGGGATGCTGCTGGAACACAGCTTCACTTTGCTGAAC
GAAGTCGGCCTACTGGAGTTCTTCCAAAATGTGATAAAAGAAACTAGGGCAGAGCCAAAA
AAGGTGACTAGTTGGGTCCTCAACACTTTTCTGGGCTATTTAAAGCAACAGAACCTCGCT
GTCAGTGAGAGTCCTGTCACACCCTCTGCACTCGCTGAGCTTCTTGACCTGCTGGACAGC
AGAACAATTTCTTCATCAGCAGCTAAACAGGTGTTTGAGGAACTGTGGAAGAGGGAAGGC
AAGACTCCAGGGCAGATTGTTTCAGAAAAGCAGCTTGAACTGATGCAGGACCAGGGGGCA
CTGGAGCAGCTCTGCCACTCTGTGATGGAGGCCCATCCTCAAGTGGTAATGGATGTGAAG
AACAGAAACCCCAGAGCTATAAATAAACTGATTGGGTTGGTCCGGAAAGCGACTCAAAGC
CGAGCAGATCCAGTCATGATAAAGGAGATCCTGGAGAAGAAGCTGTCATTGTGA
Enzyme 19 GenBank Gene ID AF026851 Link Image
Enzyme 19 GeneCard ID PET112L Link Image
Enzyme 19 GenAtlas ID PET112L Link Image
Enzyme 19 HGNC ID HGNC:8849 Link Image
Enzyme 19 Chromosome Location 4
Enzyme 19 Locus 4q27-q28
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Petruzzella V, Tiranti V, Fernandez P, Ianna P, Carrozzo R, Zeviani M: Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain. Genomics. 1998 Dec 15;54(3):494-504. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 7373
Enzyme 20 Name Neutral amino acid transporter B(0)
Enzyme 20 Synonyms
  1. ATB(0
  2. Solute carrier family 1 member 5
  3. Sodium-dependent neutral amino acid transporter type 2
  4. RD114/simian type D retrovirus receptor
  5. Baboon M7 virus receptor
Enzyme 20 Gene Name SLC1A5
Enzyme 20 Protein Sequence >Neutral amino acid transporter B(0) 
MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRANLLVLLTVV
AVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLD
PGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAGSAENAPSKEV
LDSFLDLARNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIV
FGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFA
RLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLM
MKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVT
ATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAG
LLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESV
M
Enzyme 20 Number of Residues 541
Enzyme 20 Molecular Weight 56599
Enzyme 20 Theoretical pI 5.14
Enzyme 20 GO Classification
Function
  • carboxylic acid transporter activity
  • dicarboxylic acid transporter activity
  • organic acid transporter activity
  • sodium:dicarboxylate symporter activity
  • transporter activity
Process
  • carboxylic acid transport
  • cellular physiological process
  • dicarboxylic acid transport
  • organic acid transport
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 20 General Function Energy production and conversion
Enzyme 20 Specific Function Has a broad substrate specificity, a preference for zwitterionic amino acids, and a sodium-dependence. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated amino acids, anionic amino acids, and cationic amino acids. Act as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 53-73 99-119 133-153 225-245 266-286 306-326 336-356 377-397 399-419 426-446
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 1478281 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q15758 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name AAAT_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1626 bp 
ATGGTGGCCGATCCTCCTCGAGACTCCAAGGGGCTCGCAGCGGCGGAGCCACCGCCAACG
GGGGCCTGGCAGCTGGCCTCCATCGAGGACCAAGGCGCGGCAGCAGGCGGCTACTGCGGT
TCCCGGGACCTGGTGCGCCGCTGCCTTCGAGCCAACCTGCTTGTGCTGCTGACAGTGGTG
GCCGTGGTGGCCGGCGTGGCGCTGGGACTGGGGGTGTCGGGGGCCGGGGGTGCGCTGGCG
TTGGGCCCGGGAGCGCTTGAGGCCTTCGTCTTCCCGGGCGAGCTGCTGCTGCGTCTGCTG
CGGATGATCATCTTGCCGCTGGTGGTGTGCAGCTTGATCGGCGGCGCCGCCAGCCTGGAC
CCCGGCGCGCTCGGCCGTCTGGGCGCCTGGGCGCTGCTCTTTTTCCTGGTCACCACGCTG
CTGGCGTCGGCGCTCGGAGTGGGCTTGGCGCTGGCTCTGCAGCCGGGCGCCGCCTCCGCC
GCCATCAACGCCTCCGTGGGAGCCGCGGGCAGTGCCGAAAATGCCCCCAGCAAGGAGGTG
CTCGATTCGTTCCTGGATCTTGCGAGAAATATCTTCCCTTCCAACCTGGTGTCAGCAGCC
TTTCGCTCATACTCTACCACCTATGAAGAGAGGAATATCACCGGAACCAGGGTGAAGGTG
CCCGTGGGGCAGGAGGTGGAGGGGATGAACATCCTGGGCTTGGTAGTGTTTGCCATCGTC
TTTGGTGTGGCGCTGCGGAAGCTGGGGCCTGAAGGGGAGCTGCTTATCCGCTTCTTCAAC
TCCTTCAATGAGGCCACCATGGTTCTGGTCTCCTGGATCATGTGGTACGCCCCTGTGGGC
ATCATGTTCCTGGTGGCTGGCAAGATCGTGGAGATGGAGGATGTGGGTTTACTCTTTGCC
CGCCTTGGCAAGTACATTCTGTGCTGCCTGCTGGGTCACGCCATCCATGGGCTCCTGGTA
CTGCCCCTCATCTACTTCCTCTTCACCCGCAAAAACCCCTACCGCTTCCTGTGGGGCATC
GTGACGCCGCTGGCCACTGCCTTTGGGACCTCTTCCAGTTCCGCCACGCTGCCGCTGATG
ATGAAGTGCGTGGAGGAGAATAATGGCGTGGCCAAGCACATCAGCCGTTTCATCCTGCCC
ATCGGCGCCACCGTCAACATGGACGGTGCCGCGCTCTTCCAGTGCGTGGCCGCAGTGTTC
ATTGCACAGCTCAGCCAGCAGTCCTTGGACTTCGTAAAGATCATCACCATCCTGGTCACG
GCCACAGCGTCCAGCGTGGGGGCAGCGGGCATCCCTGCTGGAGGTGTCCTCACTCTGGCC
ATCATCCTCGAAGCAGTCAACCTCCCGGTCGACCATATCTCCTTGATCCTGGCTGTGGAC
TGGCTAGTCGACCGGTCCTGTACCGTCCTCAATGTAGAAGGTGACGCTCTGGGGGCAGGA
CTCCTCCAAAATTATGTGGACCGTACGGAGTCGAGAAGCACAGAGCCTGAGTTGATACAA
GTGAAGAGTGAGCTGCCCCTGGATCCGCTGCCAGTCCCCACTGAGGAAGGAAACCCCCTC
CTCAAACACTATCGGGGGCCCGCAGGGGATGCCACGGTCGCCTCTGAGAAGGAATCAGTC
ATGTAA
Enzyme 20 GenBank Gene ID U53347 Link Image
Enzyme 20 GeneCard ID SLC1A5 Link Image
Enzyme 20 GenAtlas ID SLC1A5 Link Image
Enzyme 20 HGNC ID HGNC:10943 Link Image
Enzyme 20 Chromosome Location 19
Enzyme 20 Locus 19q13.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Kekuda R, Prasad PD, Fei YJ, Torres-Zamorano V, Sinha S, Yang-Feng TL, Leibach FH, Ganapathy V: Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line. J Biol Chem. 1996 Aug 2;271(31):18657-61. [PubMed Link Image]
  2. Rasko JE, Battini JL, Gottschalk RJ, Mazo I, Miller AD: The RD114/simian type D retrovirus receptor is a neutral amino acid transporter. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2129-34. [PubMed Link Image]
  3. Tailor CS, Nouri A, Zhao Y, Takeuchi Y, Kabat D: A sodium-dependent neutral-amino-acid transporter mediates infections of feline and baboon endogenous retroviruses and simian type D retroviruses. J Virol. 1999 May;73(5):4470-4. [PubMed Link Image]
  4. Tailor CS, Marin M, Nouri A, Kavanaugh MP, Kabat D: Truncated forms of the dual function human ASCT2 neutral amino acid transporter/retroviral receptor are translationally initiated at multiple alternative CUG and GUG codons. J Biol Chem. 2001 Jul 20;276(29):27221-30. Epub 2001 May 11. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 7884
Enzyme 21 Name Large neutral amino acids transporter small subunit 2
Enzyme 21 Synonyms
  1. L-type amino acid transporter 2
  2. hLAT2
Enzyme 21 Gene Name SLC7A8
Enzyme 21 Protein Sequence >Large neutral amino acids transporter small subunit 2 
MEEGARHRNNTEKKHPGGGESDASPEAGSGGGGVALKKEIGLVSACGIIVGNIIGSGIFV
SPKGVLENAGSVGLALIVWIVTGFITVVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGF
LRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSV
RWATRVQDIFTAGKLLALALIIIMGIVQICKGEYFWLEPKNAFENFQEPDIGLVALAFLQ
GSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYVTAMSPQELLASN
AVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVK
RCTPIPALLFTCISTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPI
KINLLFPIIYLLFWAFLLVFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFSDFI
ELLTLVSQKMCVVVYPEVERGSGTEEANEDMEEQQQPMYQPTPTKDKDVAGQPQP
Enzyme 21 Number of Residues 535
Enzyme 21 Molecular Weight 58382
Enzyme 21 Theoretical pI 5.75
Enzyme 21 GO Classification
Function
  • amine transporter activity
  • amino acid permease activity
  • amino acid transporter activity
  • amino acid-polyamine transporter activity
  • transporter activity
Process
  • amine transport
  • amino acid transport
  • cellular physiological process
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 21 General Function Amino acid transport and metabolism
Enzyme 21 Specific Function Sodium-independent, high-affinity transport of large neutral amino acids. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 40-60 72-92 113-133 155-175 189-209 231-251 268-288 310-330 362-382 388-408 424-444 447-467
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 6642960 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9UHI5 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name LAT2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1608 bp 
ATGGAAGAAGGAGCCAGGCACCGAAACAACACCGAAAAGAAACACCCAGGTGGGGGCGAG
TCGGACGCCAGCCCCGAGGCTGGTTCCGGAGGGGGCGGAGTAGCCCTGAAGAAAGAGATC
GGATTGGTCAGTGCCTGTGGTATCATCGTAGGGAACATCATCGGCTCTGGAATCTTTGTC
TCGCCAAAGGGAGTGCTGGAGAATGCTGGTTCTGTGGGCCTTGCTCTCATCGTCTGGATT
GTGACGGGCTTCATCACAGTTGTGGGAGCCCTCTGCTATGCTGAACTCGGGGTCACCATC
CCCAAATCTGGAGGTGACTACTCCTATGTCAAGGACATCTTCGGAGGACTGGCTGGGTTC
CTGAGGCTGTGGATTGCTGTGCTGGTGATCTACCCCACCAACCAGGCTGTCATCGCCCTC
ACCTTCTCCAACTACGTGCTGCAGCCGCTCTTCCCCACCTGCTTCCCCCCAGAGTCTGGC
CTTCGGCTCCTGGCTGCCATCTGCTTATTGCTCCTCACATGGGTCAACTGTTCCAGTGTG
CGGTGGGCCACCCGGGTTCAAGACATCTTCACAGCTGGGAAGCTCCTGGCCTTGGCCCTG
ATTATCATCATGGGGATTGTACAGATATGCAAAGGAGAGTACTTCTGGCTGGAGCCAAAG
AATGCATTTGAGAATTTCCAGGAACCTGACATCGGCCTCGTCGCACTGGCTTTCCTTCAG
GGCTCCTTTGCCTATGGAGGCTGGAACTTTCTGAATTACGTGACTGAGGAGCTTGTTGAT
CCCTACAAGAACCTTCCCAGAGCCATCTTCATCTCCATCCCACTGGTCACATTTGTGTAT
GTCTTTGCCAATGTCGCTTATGTCACTGCAATGTCCCCCCAGGAGCTGCTGGCATCCAAC
GCCGTCGCTGTGACTTTTGGAGAGAAGCTCCTAGGAGTCATGGCCTGGATCATGCCCATT
TCTGTTGCCCTGTCCACATTTGGAGGAGTTAATGGGTCTCTCTTCACCTCCTCTCGGCTG
TTCTTCGCTGGAGCCCGAGAGGGCCACCTTCCCAGTGTGTTGGCCATGATCCACGTGAAG
CGCTGCACCCCAATCCCAGCCCTGCTCTTCACATGCATCTCCACCCTGCTGATGCTGGTC
ACCAGCGACATGTACACACTCATCAACTACGTGGGCTTCATCAACTACCTCTTCTATGGG
GTCACGGTTGCTGGACAGATAGTCCTTCGCTGGAAGAAGCCTGATATCCCCCGCCCCATC
AAGATCAACCTGCTGTTCCCCATCATCTACTTGCTGTTCTGGGCCTTCCTGCTGGTCTTC
AGCCTGTGGTCAGAGCCGGTGGTGTGTGGCATTGGCCTGGCCATCATGCTGACAGGAGTG
CCTGTCTATTTCCTGGGTGTTTACTGGCAACACAAGCCCAAGTGTTTCAGTGACTTCATT
GAGCTGCTAACCCTGGTGAGCCAGAAGATGTGTGTGGTCGTGTACCCCGAGGTGGAGCGG
GGCTCAGGGACAGAGGAGGCTAATGAGGACATGGAGGAGCAGCAGCAGCCCATGTACCAA
CCCACTCCCACGAAGGACAAGGACGTGGCGGGGCAGCCCCAGCCCTGA
Enzyme 21 GenBank Gene ID AF171669 Link Image
Enzyme 21 GeneCard ID SLC7A8 Link Image
Enzyme 21 GenAtlas ID SLC7A8 Link Image
Enzyme 21 HGNC ID HGNC:11066 Link Image
Enzyme 21 Chromosome Location 14
Enzyme 21 Locus 14q11.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Rossier G, Meier C, Bauch C, Summa V, Sordat B, Verrey F, Kuhn LC: LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. J Biol Chem. 1999 Dec 3;274(49):34948-54. [PubMed Link Image]
  2. Borsani G, Bassi MT, Sperandeo MP, De Grandi A, Buoninconti A, Riboni M, Manzoni M, Incerti B, Pepe A, Andria G, Ballabio A, Sebastio G: SLC7A7, encoding a putative permease-related protein, is mutated in patients with lysinuric protein intolerance. Nat Genet. 1999 Mar;21(3):297-301. [PubMed Link Image]
  3. Pineda M, Fernandez E, Torrents D, Estevez R, Lopez C, Camps M, Lloberas J, Zorzano A, Palacin M: Identification of a membrane protein, LAT-2, that Co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids. J Biol Chem. 1999 Jul 9;274(28):19738-44. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 7918
Enzyme 22 Name L-glutaminase
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name Not Available
Enzyme 22 Protein Sequence >L-glutaminase 
MRSMKALQKALSRAGSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQD
HDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQ
ESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVA
AYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHK
FVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAG
NEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESG
SVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGA
ILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGA
EIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE
ACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLES
MV
Enzyme 22 Number of Residues 602
Enzyme 22 Molecular Weight 66324
Enzyme 22 Theoretical pI 7.32
Enzyme 22 GO Classification
Function
  • catalytic activity
  • glutaminase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 22 General Function Amino acid transport and metabolism
Enzyme 22 Specific Function L-glutamine + H(2)O = L-glutamate + NH(3)
Enzyme 22 Pathways
Enzyme 22 Reactions
  • L-glutamine + H2O = L-glutamate + NH3
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 29029569 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q8IX91 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name Q8IX91_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1809 bp 
ATGCGCTCCATGAAGGCTCTGCAGAAGGCCCTGAGCCGGGCTGGCAGTCACTGCGGGCGA
GGAGGCTGGGGTCACCCGAGCCGGAGCCCCCTCCTTGGCGGGGGCGTCCGGCACCACCTC
AGTGAGGCCGCGGCGCAGGGCAGAGAGACGCCACACAGCCACCAGCCGCAGCACCAGGAT
CATGATTCATCAGAAAGTGGCATGCTGTCCCGCCTGGGTGATTTGCTCTTTTACACTATT
GCTGAAGGACAGGAACGAATCCCTATCCACAAGTTCACCACTGCACTAAAGGCCACTGGA
CTGCAGACATCAGATCCTCGGCTCCGAGACTGCATGAGCGAGATGCACCGCGTGGTCCAA
GAGTCCAGTAGTGGTGGCCTCTTGGACCGAGATCTCTTCCGAAAGTGTGTGAGCAGCAAC
ATTGTGCTCCTGACCCAGGCATTCCGAAAGAAGTTTGTCATTCCTGATTTTGAGGAGTTC
ACGGGCCATGTGGATCGCATCTTTGAGGATGTCAAAGAGCTCACTGGAGGCAAAGTGGCA
GCCTACATCCCTCAGCTGGCCAAGTCAAACCCAGACCTGTGGGGTGTCTCCCTGTGCACT
GTGGATGGTCAACGGCACTCTGTGGGCCACACAAAGATCCCCTTCTGCCTGCAGTCCTGT
GTGAAGCCCCTCACCTATGCCATCTCCATAAGCACCCTAGGCACTGACTACGTGCACAAG
TTTGTGGGCAAAGAGCCAAGTGGCCTGCGCTACAACAAGCTCTCCCTCAATGAGGAAGGA
ATCCCCCATAACCCCATGGTCAATGCTGGTGCCATTGTTGTCAGCTCCCTGATCAAGATG
GACTGTAACAAAGCAGAGAAGTTTGATTTTGTGTTGCAGTATCTCAACAAAATGGCTGGG
AATGAATACATGGGTTTCAGCAATGCCACATTCCAGTCAGAGAAGGAAACAGGGGATCGG
AATTATGCCATCGGCTATTATCTCAAGGAAAAGAAGTGCTTTCCTAAGGGGGTGGACATG
ATGGCTGCCCTTGATCTCTACTTCCAGCTGTGTTCTGTGGAGGTCACTTGTGAATCAGGC
AGTGTCATGGCAGCCACCCTCGCCAACGGTGGGATCTGCCCCATCACAGGCGAGAGTGTG
CTGAGTGCTGAAGCAGTGCGCAACACCCTCAGCCTCATGCATTCCTGCGGCATGTATGAC
TTCTCTGGCCAGTTTGCCTTCCACGTGGGCCTGCCAGCCAAGTCAGCTGTATCAGGAGCC
ATCCTCCTGGTGGTACCCAATGTCATGGGAATGATGTGCCTGTCACCCCCATTGGACAAG
CTGGGGAACAGCCATAGGGGGACCAGCTTCTGCCAGAAGTTGGTGTCTCTCTTCAATTTC
CACAACTATGACAACCTGAGGCACTGTGCTCGGAAGTTAGACCCACGGCGTGAAGGGGCA
GAAATTCGGAACAAGACTGTGGTCAACCTGTTATTTGCTGCCTATAGTGGCGATGTCTCA
GCTCTTCGAAGGTTTGCCTTGTCAGCCATGGATATGGAACAGAAAGACTATGACTCGCGC
ACAGCTCTGCATGTTGCTGCAGCTGAAGGACACATCGAAGTTGTTAAATTCCTGATCGAG
GCTTGCAAAGTGAATCCTTTTGCCAAGGACAGGTGGGGCAACATTCCCCTGGATGATGCT
GTGCAGTTCAACCATCTGGAGGTGGTCAAACTGCTTCAAGATTACCAGGACTCCTACACA
CTCTCTGAAACTCAGGCTGAGGCAGCAGCTGAGGCCCTGTCCAAAGAGAACTTAGAAAGC
ATGGTATGA
Enzyme 22 GenBank Gene ID AF348119 Link Image
Enzyme 22 GeneCard ID Not Available
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID HGNC:29570 Link Image
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs Not Available
Enzyme 22 General References
  1. Perez-Gomez C, Mates JM, Gomez-Fabre PM, del Castillo-Olivares A, Alonso FJ, Marquez J: Genomic organization and transcriptional analysis of the human l-glutaminase gene. Biochem J. 2003 Mar 15;370(Pt 3):771-84. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 8562
Enzyme 23 Name System N amino acid transporter 1
Enzyme 23 Synonyms
  1. SN1
  2. N-system amino acid transporter 1
  3. Solute carrier family 38 member 3
Enzyme 23 Gene Name SLC38A3
Enzyme 23 Protein Sequence >System N amino acid transporter 1 
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 23 Number of Residues 504
Enzyme 23 Molecular Weight 55774
Enzyme 23 Theoretical pI 8.01
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Amino acid transport and metabolism
Enzyme 23 Specific Function Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-111
Enzyme 23 Transmembrane Regions
  • 83-103 106-126 144-164 187-207 213-233 324-344 366-386 408-428 431-451 471-491
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID Q99624 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name S38A3_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence Not Available
Enzyme 23 GenBank Gene ID AF244548 Link Image
Enzyme 23 GeneCard ID SLC38A3 Link Image
Enzyme 23 GenAtlas ID SLC38A3 Link Image
Enzyme 23 HGNC ID HGNC:18044 Link Image
Enzyme 23 Chromosome Location 3
Enzyme 23 Locus 3p21.3
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Fei YJ, Sugawara M, Nakanishi T, Huang W, Wang H, Prasad PD, Leibach FH, Ganapathy V: Primary structure, genomic organization, and functional and electrogenic characteristics of human system N 1, a Na+- and H+-coupled glutamine transporter. J Biol Chem. 2000 Aug 4;275(31):23707-17. [PubMed Link Image]
  2. Lerman MI, Minna JD: The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium. Cancer Res. 2000 Nov 1;60(21):6116-33. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 8813
Enzyme 24 Name Glutamine-dependent NAD(+) synthetase
Enzyme 24 Synonyms
  1. NAD(+synthase [glutamine-hydrolyzing]
  2. NAD(+synthetase 1
Enzyme 24 Gene Name NADSYN1
Enzyme 24 Protein Sequence >Glutamine-dependent NAD(+) synthetase 
MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYES
DTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANE
GNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWT
PHSPHIDMGLDGVEIITNASGSHHVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRL
YYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPR
VKVDFALSCHEDLLAPISEPIEWKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGV
DSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQISYTPQDPRDLCGRILTTCYMAS
KNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLA
LQNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIG
GISKTDLRAFVQFCIQRFQLPALQSILLAPATAELEPLADGQVSQTDEEDMGMTYAELSV
YGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFSKYSMNRHKMTTLTPAYHAE
NYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEPQSLDGVD
Enzyme 24 Number of Residues 706
Enzyme 24 Molecular Weight 79295
Enzyme 24 Theoretical pI 6.46
Enzyme 24 GO Classification
Function
  • ATP binding
  • NAD+ synthase (glutamine-hydrolyzing) activity
  • adenyl nucleotide binding
  • binding
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • NAD biosynthesis
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • nitrogen compound metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
Component
—
Enzyme 24 General Function Coenzyme transport and metabolism
Enzyme 24 Specific Function ATP + deamido-NAD(+) + L-glutamine + H(2)O = AMP + diphosphate + NAD(+) + L-glutamate
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals Not Available
Enzyme 24 Transmembrane Regions Not Available
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID Q6IA69 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name NADE1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AB091316 Link Image
Enzyme 24 GeneCard ID NADSYN1 Link Image
Enzyme 24 GenAtlas ID NADSYN1 Link Image
Enzyme 24 HGNC ID HGNC:29832 Link Image
Enzyme 24 Chromosome Location 11
Enzyme 24 Locus 11q13.4
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, Tsuchiya M: Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. J Biol Chem. 2003 Mar 28;278(13):10914-21. Epub 2003 Jan 23. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 8876
Enzyme 25 Name CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name CAD
Enzyme 25 Protein Sequence >CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase 
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNY
GIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVD
TRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILA
LDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVL
SEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVE
TDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA
TAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAI
KALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQT
ALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQ
AQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEI
EYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLG
IVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRN
SVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKAL
RMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRM
KRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAV
KQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQ
QLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLP
NNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT
VGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAV
ASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN
LQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVG
VKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIG
SYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSI
LEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL
GQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMV
CAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLN
ETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEE
ILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVI
DCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIF
HLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVL
VPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASD
PGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHS
LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSF
AAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRR
PVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVS
LRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA
CFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLAT
VLGRF
Enzyme 25 Number of Residues 2225
Enzyme 25 Molecular Weight 242987
Enzyme 25 Theoretical pI 6.42
Enzyme 25 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • amine binding
  • amino acid binding
  • aspartate carbamoyltransferase activity
  • binding
  • carbamoyl-phosphate synthase activity
  • carboxyl- and carbamoyltransferase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • 'de novo' pyrimidine base biosynthesis
  • amino acid and derivative metabolism
  • amino acid metabolism
  • arginine biosynthesis
  • arginine metabolism
  • biosynthesis
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • nitrogen compound metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base biosynthesis
  • pyrimidine base metabolism
  • urea cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 25 General Function Amino acid transport and metabolism
Enzyme 25 Specific Function This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)
Enzyme 25 Pathways
Enzyme 25 Reactions
  • 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals Not Available
Enzyme 25 Transmembrane Regions Not Available
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 1228049 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P27708 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PYR1_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >6678 bp 
ATGGCGGCCCTAGTGTTGGAGGACGGGTCGGTCCTGCGGGGCCAGCCCTTTGGGGCCGCC
GTGTCGACTGCCGGGGAAGTGGTGTTTCAAACCGGCATGGTCGGCTACCCCGAGGCCCTC
ACTGATCCCTCCTACAAGGCACAGATCTTAGTGCTCACCTATCCTCTGATCGGCAACTAT
GGCATCCCCCCAGATGAAATGGATGAGTTCGGTCTCTGCAAGTGGTTTGAATCCTCGGGC
ATCCACGTAGCAGCACTGGTAGTGGGAGAGTGCTGTCCTACTCCCAGCCACTGGAGTGCC
ACCCGCACCCTGCATGAGTGGCTGCAGCAGCATGGCATCCCTGGCTTGCAAGGAGTAGAC
ACTCGGGAGCTGACCAAGAAGTTGCGGGAACAGGGGTCTCTGCTGGGGAAGCTGGTCCAG
AATGGAACAGAACCTTCATCCCTGCCATTCTTGGACCCCAATGCCCGCCCCCTGGTACCA
GAGGTCTCCATTAAGACTCCACGGGTATTCAATACAGGGGGTGCCCCTCGGATCCTTGCT
TTGGACTGTGGCCTCAAGTATAATCAGATCCGATGCCTCTGCCAGCGTGGGGCTGAGGTC
ACTGTGGTACCCTGGGACCATGCACTAGACAGCCAAGAGTATGAGGGTCTCTTCTTAAGT
AATGGGCCTGGTGACCCTGCCTCCTATCCCAGTGTCGTATCCACACTGAGCCGTGTTTTA
TCTGAGCCTAATCCCCGACCTGTCTTTGGGATCTGCCTGGGACACCAGCTATTGGCCTTA
GCCATTGGGGCCAAGACTTACAAGATGAGATATGGGAACCGAGGCCATAACCAGCCCTGC
TTGTTGGTGGGCTCTGGGCGCTGCTTTCTGACATCCCAGAACCATGGGTTTGCTGTGGAG
ACAGACTCACTGCCAGCAGACTGGGCTCCTCTCTTCACCAACGCCAATGATGGTTCCAAT
GAAGGCATTGTGCACAACAGCTTGCCTTTCTTCAGTGTCCAGTTTCACCCAGAGCACCAA
GCTGGCCCTTCAGATATGGAACTGCTTTTCGATATCTTTCTGGAAACTGTGAAAGAGGCC
ACAGCTGGGAACCCTGGGGGCCAGACAGTTAGAGAGCGGCTGACTGAGCGCCTCTGTCCC
CCTGGGATTCCCACTCCCGGCTCTGGACTTCCACCACCACGAAAGGTTCTGATCCTGGGC
TCAGGGGGCCTCTCCATTGGCCAAGCTGGAGAATTTGACTACTCGGGCTCTCAGGCAATT
AAGGCCCTGAAGGAGGAAAACATCCAGACGTTGCTGATCAACCCCAATATTGCCACAGTG
CAGACCTCCCAGGGGCTGGCCGACAAGGTCTATTTTCTTCCCATAACACCTCATTATGTA
ACCCAGGTGATACGTAATGAACGCCCCGATGGTGTGTTACTGACTTTTGGGGGCCAGACT
GCTCTGAACTGTGGTGTGGAGCTGACCAAGGCCGGGGTGCTGGCTCGGTATGGGGTCCGG
GTCCTGGGCACAACAGTGGAGACCATTGAGCTGACCGAGGATCGACGGGCCTTTGCTGCC
AGAATGGCAGAGATCGGAGAGCATGTGGCCCCGAGCGAGGCAGGAAATTCTCTTGAACAG
GCCCAGGCAGCCGCTGAACGGCTGGGGTACCCTGTGCTAGTGCGTGCAGCCTTTGCCGTG
GGTGGCCTGGGCTCTGGCTTTGCCTCTAACAGGGAGGAGCTCTCTGCTCTCGTGGCCCCA
GCTTTTGCCCATACCAGCCAAGTGCTAGTAGACAAGTCTCTGAAGGGATGGAAGGAGATT
GAGTACGAGGTGGTGAGAGACGCCTATGGCAACTGTGTCACGGTGTGTAACATGGAGAAC
TTGGACCCACTGGGCATCCACACTGGTGAGTCCATAGTGGTGGCCCCTAGCCAGACACTG
AATGACAGGGAGTATCAGCTCCTGAGGCAGACAGCTATCAAGGTGACCCAGCACCTGGGA
ATTGTTGGGGAGTGCAATGTGCAGTATGCCTTGAACCCTGAGTCTGAGCAGTATTACATC
ATTGAAGTGAATGCCAGGCTCTCTCGCAGCTCTGCCCTGGCCAGTAAGGCCACAGGTTAT
CCACTGGCTTATGTGGCAGCCAAGCTAGCATTGGGCATCCCTTTGCCTGAGCTCAGGAAC
TCTGTGACAGGGGGTACAGCAGCCTTTGAACCCAGCGTGGATTATTGTGTGGTGAAGATT
CCTCGATGGGACCTTAGCAAGTTCCTGCGAGTCAGCACAAAGATTGGGAGCTGCATGAAG
AGCGTTGGTGAAGTCATGGGCATTGGGCGTTCATTTGAGGAGGCCTTCCAGAAGGCCCTG
CGCATGGTGGATGAGAACTGTGTGGGCTTTGATCACACAGTGAAACCAGTCAGCGATATG
GAGTTGGAGACTCCAACAGATAAGCGGATTTTTGTGGTGGCAGCTGCTTTGTGGGCTGGT
TATTCAGTGGACCGCCTGTATGAGCTCACACGCATCGACCGCTGGTTCCTGCACCGAATG
AAGCGTATCATCGCACATGCCCAGCTGCTAGAACAACACCGTGGACAGCCTTTGCCGCCA
GACCTGCTGCAACAGGCCAAGTGTCTTGGCTTCTCAGACAAACAGATTGCCCTTGCAGTT
CTGAGCACAGAGCTGGCTGTTCGCAAGCTGCGTCAGGAACTGGGGATCTGTCCAGCAGTG
AAACAGATTGACACAGTTGCAGCTGAGTGGCCAGCCCAGACAAATTACCTATACCTAACG
TATTGGGGCACCACCCATGACCTCACCTTTCGAACACCTCATGTCCTAGTCCTTGGCTCT
GGCGTCTACCGTATTGGCTCCAGTGTTGAGTTTGACTGGTGTGCTGTAGGCTGCATCCAG
CAGCTCCGAAAGATGGGATATAAGACCATCATGGTGAACTATAACCCAGAGACAGTCAGC
ACCGACTATGACATGTGTGATCGACTCTACTTTGATGAGATCTCTTTTGAGGTGGTGATG
GACATCTATGAGCTCGAGAACCCTGAAGGTGTGATCCTATCCATGGGTGGACAGCTGCCC
AACAACATGGCCATGGCGTTGCATCGGCAGCAGTGCCGGGTGCTGGGCACCTCCCCTGAA
GCCATTGACTCGGCTGAGAACCGTTTCAAGTTTTCCCGGCTCCTTGACACCATTGGTATC
AGCCAGCCTCAGTGGAGGGAGCTCAGTGACCTCGAGTCTGCTCGCCAATTCTGCCAGACC
GTGGGGTACCCCTGTGTGGTGCGCCCCTCCTATGTGCTGAGCGGTGCTGCTATGAATGTG
GCCTACGCGGATGGAGACCTGGAGCGCTTCCTGAGCAGCGCAGCAGCCGTCTCCAAAGAG
CATCCCGTGGTCATCTCCAAGTTCATCCAGGAGGCTAAGGAGATTGACGTGGATGCCGTG
GCCTCTGATGGTGTGGTGGCAGCCATCGCCATCTCTGAGCATGTGGAGAATGCAGGTGTG
CATTCAGGTGATGCGACGCTGGTGACCCCCCCACAAGATATCACTGCCAAAACCCTGGAG
CGGATCAAAGCCATTGTGCATGCTGTGGGCCAGGAGCTACAGGTCACAGGACCCTTCAAT
CTGCAGCTCATTGCCAAGGATGACCAGCTGAAAGTTATTGAATGCAACGTACGTGTCTCT
CGCTCCTTCCCCTTCGTTTCCAAGACACTGGGTGTGGACCTAGTAGCCTTGGCCACGCGG
GTCATCATGGGGGAAGAAGTGGAACCTGTGGGGCTAATGACTGGTTCTGGAGTCGTGGGA
GTAAAGGTGCCTCAGTTCTCCTTCTCCCGCTTGGCGGGTGCTGACGTGGTGTTGGGTGTG
GAAATGACCAGTACTGGGGAGGTGGCCGGCTTTGGGGAGAGCCGCTGTGAGGCATACCTC
AAGGCCATGCTAAGCACTGGCTTTAAGATCCCCAAGAAGAATATCCTGCTGACCATTGGC
AGCTATAAGAACAAAAGCGAGCTGCTCCCAACTGTGCGGCTACTGGAGAGCCTGGGCTAC
AGCCTCTATGCCAGTCTCGGCACAGCTGACTTCTACACTGAGCATGGCGTCAAGGTAACA
GCTGTGGACTGGCACTTTGAGGAGGCTGTGGATGGTGAGTGCCCACCACAGCGGAGCATC
CTGGAGCAGCTAGCTGAGAAAAACTTTGAGCTGGTGATTAACCTGTCAATGCGTGGAGCT
GGGGGCCGGCGTCTCTCCTCCTTTGTCACCAAGGGCTACCGCACCCGACGCTTGGCCGCT
GACTTCTCCGTGCCCCTAATCATCGATATCAAGTGCACCAAACTCTTTGTGGAGGCCCTA
GGCCAGATCGGGCCAGCCCCTCCTTTGAAGGTGCATGTTGACTGTATGACCTCCCAAAAG
CTTGTGCGACTGCCGGGATTGATTGATGTCCATGTGCACCTGCGGGAACCAGGTGGGACA
CATAAGGAGGACTTTGCTTCAGGCACAGCCGCTGCCCTGGCTGGGGGTATCACCATGGTG
TGTGCCATGCCTAATACCCGGCCCCCCATCATTGACGGCCCTGCTCTGGCCCTGGCCCAG
AAGCTGGCAGAGGCTGGCGCCCGGTGCGACTTTGCGCTATTCCTTGGGGCCTCGTCTGAA
AATGCAGGAACCTTGGGCACCGTGGCCGGGTCTGCAGCCGGGCTGAAGCTTTACCTCAAT
GAGACCTTCTCTGAGCTGCGGCTGGACAGCGTGGTCCAGTGGATGGAGCATTTCGAGACA
TGGCCCTCCCACCTCCCCATTGTGGCTCACGCAGAGCAGCAAACCGTGGCTGCTGTCCTC
ATGGTGGCTCAGCTCACTCAGCGCTCAGTGCACATATGTCACGTGGCACGGAAGGAGGAG
ATCCTGCTAATTAAAGCTGCAAAGGCACGGGGCTTGCCAGTGACCTGCGAGGTGGCTCCC
CACCACCTGTTCCTAAGCCATGATGACCTGGAGCGCCTGGGGCCTGGGAAGGGGGAGGTC
CGGCCTGAGCTTGGCTCCCGCCAGGATGTGGAAGCCCTGTGGGAGGACATGGCTGTCATC
GACTGCTTTGCCTCAGACCATGCTCCCCATACCTTGGAGGAGAAGTGTGGGTCCAGGCCC
CCACCTGGGTTCCCAGGGTTAGAGACCATGCTGCCACTACTCCTGACGGCTGTAAGCGAG
GGCCGGCTCAGCCTGGACGACCTGCTGCAGCGATTGCACCACAATCCTCGGCGCATCTTT
CACCTGCCCCCGCAGGAGGACACCTATGTGGAGGTGGATCTGGAGCATGAGTGGACAATT
CCCAGCCACATGCCCTTCTCCAAGGCCCACTGGACACCTTTTGAAGGGCAGAAAGTGAAG
GGCACCGTCCGCCGTGTGGTCCTGCGAGGGGAGGTTGCCTATATCGATGGGCAGGTTCTG
GTACCCCCGGGCTATGGACAGGATGTACGGAAGTGGCCACAGGGGGCTGTTCCTCAGCTC
CCACCCTCAGCCCCTGCCACTAGTGAGATGACCACGACACCTGAAAGACCCCGCCGTGGC
ATCCCAGGGCTTCCTGATGGCCGCTTCCATCTGCCGCCCCGAATCCATCGAGCCTCCGAC
CCAGGTTTGCCAGCTGAGGAGCCAAAGGAGAAGTCCTCTCGGAAGGTAGCCGAGCCAGAG
CTGATGGGAACCCCTGATGGCACCTGCTACCCTCCACCACCAGTACCGAGACAGGCATCT
CCCCAGAACCTGGGGACCCCTGGCTTGCTGCACCCCCAGACCTCACCCCTGCTGCACTCA
TTAGTGGGCCAACATATCCTGTCCGTCCAGCAGTTCACCAAGGATCAGATGTCTCACCTG
TTCAATGTGGCACACACACTGCGTATGATGGTGCAGAAGGAGCGGAGCCTCGACATCCTG
AAGGGGAAGGTCATGGCCTCCATGTTCTATGAAGTGAGCACACGGACCAGCAGCTCCTTT
GCAGCAGCCATGGCCCGGCTGGGAGGTGCTGTGCTCAGCTTCTCGGAAGCCACATCGTCC
GTCCAGAAGGGCGAATCCCTGGCTGACTCCGTGCAGACCATGAGCTGCTATGCCGACGTC
GTCGTGCTCCGGCACCCCCAGCCTGGAGCAGTGGAGCTGGCCGCCAAGCACTGCCGGAGG
CCAGTGATCAATGCTGGGGATGGGGTCGGAGAGCACCCCACCCAGGCCCTGCTGGACATC
TTCACCATCCGTGAGGAGCTGGGAACTGTCAATGGCATGACGATCACGATGGTGGGTGAC
CTGAAGCACGGACGCACAGTACATTCCCTGGCCTGCCTGCTCACCCAGTATCGTGTCAGC
CTGCGCTACGTGGCACCTCCCAGCCTGCGCATGCCACCCACTGTGCGGGCCTTCGTGGCC
TCCCGCGGCACCAAGCAGGAGGAATTCGAGAGCATTGAGGAGGCGCTGCCTGACACTGAT
GTGCTCTACATGACTCGAATCCAGAAGGAACGATTTGGCTCTACCCAGGAGTACGAAGCT
TGCTTTGGTCAGTTCATCCTCACTCCCCACATCATGACCCGGGCCAAGAAGAAGATGGTG
GTGATGCACCCGATGCCCCGTGTCAACGAGATAAGCGTGGAAGTGGACTCGGATCCCCGC
GCAGCCTACTTCCGCCAGGCTGAGAACGGCATGTACATCCGCATGGCTCTGTTAGCCACC
GTGCTGGGCCGTTTCTAG
Enzyme 25 GenBank Gene ID D78586 Link Image
Enzyme 25 GeneCard ID CAD Link Image
Enzyme 25 GenAtlas ID CAD Link Image
Enzyme 25 HGNC ID HGNC:1424 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 2p22-p21
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Iwahana H, Fujimura M, Ii S, Kondo M, Moritani M, Takahashi Y, Yamaoka T, Yoshimoto K, Itakura M: Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis. Biochem Biophys Res Commun. 1996 Feb 6;219(1):249-55. [PubMed Link Image]
  2. Davidson JN, Rao GN, Niswander L, Andreano C, Tamer C, Chen KC: Organization and nucleotide sequence of the 3' end of the human CAD gene. DNA Cell Biol. 1990 Nov;9(9):667-76. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 13038
Enzyme 26 Name cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase
Enzyme 26 Synonyms
  1. PPAT, mRNA
  2. Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
Enzyme 26 Gene Name PPAT
Enzyme 26 Protein Sequence >cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase 
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Enzyme 26 Number of Residues 517
Enzyme 26 Molecular Weight 57400
Enzyme 26 Theoretical pI 6.74
Enzyme 26 GO Classification Not Available
Enzyme 26 General Function Nucleotide transport and metabolism
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function Not Available
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 158255320 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A8K4H7 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A8K4H7_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AK290942 Link Image
Enzyme 26 GeneCard ID A8K4H7 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 13039
Enzyme 27 Name cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase
Enzyme 27 Synonyms
  1. GMPS, mRNA
  2. Guanine monphosphate synthetase, isoform CRA_b
Enzyme 27 Gene Name GMPS
Enzyme 27 Protein Sequence >cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase 
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 27 Number of Residues 693
Enzyme 27 Molecular Weight 76716
Enzyme 27 Theoretical pI 6.86
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Nucleotide transport and metabolism
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function Not Available
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 158256440 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID A8K639 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name A8K639_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AK291504 Link Image
Enzyme 27 GeneCard ID A8K639 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 13040
Enzyme 28 Name Glutamine synthetase
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name PIG59
Enzyme 28 Protein Sequence >Glutamine synthetase 
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN
Enzyme 28 Number of Residues 373
Enzyme 28 Molecular Weight 42064
Enzyme 28 Theoretical pI Not Available
Enzyme 28 GO Classification Not Available
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions
  • ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID A8YXX4 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name A8YXX4_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID Not Available
Enzyme 28 GeneCard ID A8YXX4 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 15222
Enzyme 29 Name Putative uncharacterized protein GFPT1
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name GFPT1
Enzyme 29 Protein Sequence >Putative uncharacterized protein GFPT1 
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLI
KKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIV
IHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQ
LEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTGKDKKGSCNLSR
VDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGD
HPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHI
KEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFL
SQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTS
QFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSV
LIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYA
KCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHL
AVLRGYDVDFPRNLAKSVTVE
Enzyme 29 Number of Residues 681
Enzyme 29 Molecular Weight 76760
Enzyme 29 Theoretical pI 6.84
Enzyme 29 GO Classification
Function
  • binding
  • carbohydrate binding
  • catalytic activity
  • glutamine-fructose-6-phosphate transaminase (isomerizing) activity
  • sugar binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • carbohydrate biosynthesis
  • carbohydrate metabolism
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 29 General Function Cell wall/membrane/envelope biogenesis
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 62822278 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q53QE6 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name Q53QE6_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >2046 bp 
ATGTGTGGTATATTTGCTTACTTAAACTACCATGTTCCTCGAACGAGACGAGAAATCCTG
GAGACCCTAATCAAAGGCCTTCAGAGACTGGAGTACAGAGGATATGATTCTGCTGGTGTG
GGATTTGATGGAGGCAATGATAAAGATTGGGAAGCCAATGCCTGCAAAATCCAGCTTATT
AAGAAGAAAGGAAAAGTTAAGGCACTGGATGAAGAAGTTCACAAGCAACAAGATATGGAT
TTGGATATAGAATTTGATGTACACCTTGGAATAGCTCATACCCGTTGGGCAACACATGGA
GAACCCAGTCCTGTCAATAGCCACCCCCAGCGCTCTGATAAAAATAATGAATTTATCGTT
ATTCACAATGGAATCATCACCAACTACAAAGACTTGAAAAAGTTTTTGGAAAGCAAAGGC
TATGACTTCGAATCTGAAACAGACACAGAGACAATTGCCAAGCTCGTTAAGTATATGTAT
GACAATCGGGAAAGTCAAGATACCAGCTTTACTACCTTGGTGGAGAGAGTTATCCAACAA
TTGGAAGGTGCTTTTGCACTTGTGTTTAAAAGTGTTCATTTTCCCGGGCAAGCAGTTGGC
ACAAGGCGAGGTAGCCCTCTGTTGATTGGTGTACGGAGTGAACATAAACTTTCTACTGAT
CACATTCCTATACTCTACAGAACAGGCAAAGACAAGAAAGGAAGCTGCAATCTCTCTCGT
GTGGACAGCACAACCTGCCTTTTCCCGGTGGAAGAAAAAGCAGTGGAGTATTACTTTGCT
TCTGATGCAAGTGCTGTCATAGAACACACCAATCGCGTCATCTTTCTGGAAGATGATGAT
GTTGCAGCAGTAGTGGATGGACGTCTTTCTATCCATCGAATTAAACGAACTGCAGGAGAT
CACCCCGGACGAGCTGTGCAAACACTCCAGATGGAACTCCAGCAGATCATGAAGGGCAAC
TTCAGTTCATTTATGCAGAAGGAAATATTTGAGCAGCCAGAGTCTGTCGTGAACACAATG
AGAGGAAGAGTCAACTTTGATGACTATACTGTGAATTTGGGTGGTTTGAAGGATCACATA
AAGGAGATCCAGAGATGCCGGCGTTTGATTCTTATTGCTTGTGGAACAAGTTACCATGCT
GGTGTAGCAACACGTCAAGTTCTTGAGGAGCTGACTGAGTTGCCTGTGATGGTGGAACTA
GCAAGTGACTTCCTGGACAGAAACACACCAGTCTTTCGAGATGATGTTTGCTTTTTCCTT
AGTCAATCAGGTGAGACAGCAGATACTTTGATGGGTCTTCGTTACTGTAAGGAGAGAGGA
GCTTTAACTGTGGGGATCACAAACACAGTTGGCAGTTCCATATCACGGGAGACAGATTGT
GGAGTTCATATTAATGCTGGTCCTGAGATTGGTGTGGCCAGTACAAAGGCTTATACCAGC
CAGTTTGTATCCCTTGTGATGTTTGCCCTTATGATGTGTGATGATCGGATCTCCATGCAA
GAAAGACGCAAAGAGATCATGCTTGGATTGAAACGGCTGCCTGATTTGATTAAGGAAGTA
CTGAGCATGGATGACGAAATTCAGAAACTAGCAACAGAACTTTATCATCAGAAGTCAGTT
CTGATAATGGGACGAGGCTATCATTATGCTACTTGTCTTGAAGGGGCACTGAAAATCAAA
GAAATTACTTATATGCACTCTGAAGGCATCCTTGCTGGTGAATTGAAACATGGCCCTCTG
GCTTTGGTGGATAAATTGATGCCTGTGATCATGATCATCATGAGAGATCACACTTATGCC
AAGTGTCAGAATGCTCTTCAGCAAGTGGTTGCTCGGCAGGGGCGGCCTGTGGTAATTTGT
GATAAGGAGGATACTGAGACCATTAAGAACACAAAAAGAACGATCAAGGTGCCCCACTCA
GTGGACTGCTTGCAGGGCATTCTCAGCGTGATCCCTTTACAGTTGCTGGCTTTCCACCTT
GCTGTGCTGAGAGGCTATGATGTTGATTTCCCACGGAATCTTGCCAAATCTGTGACTGTA
GAGTGA
Enzyme 29 GenBank Gene ID AC114772 Link Image
Enzyme 29 GeneCard ID Q53QE6 Link Image
Enzyme 29 GenAtlas ID GFPT1 Link Image
Enzyme 29 HGNC ID HGNC:4241 Link Image
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 15223
Enzyme 30 Name cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name Not Available
Enzyme 30 Protein Sequence >cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA 
MSPVLHFYVRPSGHEGAAPGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKL
MWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVE
TTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEG
RLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLH
VDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQG
LRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGY
NLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREW
IKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLD
FGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTS
RFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVL
VDDRECPVRRNGQGDAPPTPLPTPVDLELGWVLGKMPRKEFFLQRKPPMLQPLALPPGLS
VHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIG
AATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAA
LADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTP
DLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLK
DRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPD
LAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDR
LQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMA
DAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAG
AELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLHHNLSG
RYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWA
DDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTS
PWLQLFINARNWTLEGSC
Enzyme 30 Number of Residues 1338
Enzyme 30 Molecular Weight 144645
Enzyme 30 Theoretical pI 5.60
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Nucleotide transport and metabolism
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function Not Available
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 158259069 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID A8K9T9 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name A8K9T9_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >4017 bp 
ATGTCCCCAGTCCTTCACTTCTATGTTCGTCCCTCTGGCCATGAGGGGGCAGCCCCTGGA
CACACTCGGAGGAAACTGCAAGGGAAACTGCCAGAGCTGCAGGGCGTCGAGACTGAACTG
TGCTACAACGTGAACTGGACAGCTGAGGCCCTCCCCAGTGCTGAGGAGACAAAGAAGCTG
ATGTGGCTGTTTGGTTGCCCCTTACTGCTGGATGATGTTGCTCGGGAGTCCTGGCTCCTT
CCTGGCTCCAATGACCTGCTGCTGGAGGTCGGGCCCAGGCTGAACTTCTCCACCCCAACA
TCCACCAACATCGTGTCAGTGTGCCGCGCCACTGGGCTGGGGCCTGTGGATCGTGTGGAG
ACCACCCGGCGCTACCGGCTCTCGTTTGCCCACCCCCCGTCAGCTGAGGTGGAAGCCATT
GCTCTGGCTACCCTGCACGACCGGATGACAGAGCAGCACTTCCCCCATCCCATCCAGAGT
TTCTCCCCTGAGAGCATGCCGGAACCCCTCAATGGCCCTATCAATATACTGGGTGAGGGC
CGGCTTGCGCTGGAGAAGGCCAACCAGGAGCTTGGTCTGGCTTTAGACTCTTGGGACCTA
GACTTCTACACCAAGCGCTTCCAGGAGCTACAGCGGAACCCGAGCACTGTGGAGGCCTTT
GACTTGGCGCAGTCCAATAGCGAGCACAGCCGACACTGGTTCTTCAAGGGCCAGCTCCAC
GTGGATGGGCAGAAGCTGGTGCACTCACTGTTTGAGTCCATCATGAGCACCCAGGAATCC
TCGAACCCCAACAACGTCCTCAAATTCTGTGATAACAGCAGTGCAATCCAGGGAAAGGAA
GTCCGATTCCTACGGCCTGAGGACCCCACACGGCCAAGCCGCTTCCAGCAACAGCAAGGG
CTGAGACATGTTGTCTTCACAGCAGAGACTCACAACTTTCCCACAGGAGTATGCCCCTTT
AGTGGTGCAACCACTGGCACAGGGGGCCGGATTCGAGATGTCCAGTGCACAGGCCGCGGG
GCCCACGTGGTGGCTGGCACTGCCGGCTATTGCTTTGGAAATCTGCATATTCCAGGTTAC
AATCTGCCCTGGGAGGATCCAAGCTTCCAGTATCCTGGGAATTTTGCCCGGCCCCTGGAG
GTTGCCATTGAAGCCAGTAATGGAGCTTCTGACTATGGCAACAAGTTTGGGGAACCAGTG
CTGGCTGGCTTCGCCCGCTCCTTGGGCCTCCAGCTCCCAGACGGCCAGCGGCGTGAGTGG
ATCAAGCCCATCATGTTTAGTGGGGGCATTGGGTCCATGGAAGCTGACCACATAAGCAAG
GAGGCCCCAGAGCCAGGCATGGAAGTTGTAAAGGTTGGAGGTCCCGTCTACAGGATTGGA
GTTGGAGGTGGAGCTGCTTCATCTGTGCAGGTGCAGGGAGATAACACCAGTGACCTGGAC
TTTGGGGCTGTGCAGCGAGGAGACCCGGAGATGGAACAGAAGATGAACCGTGTGATCAGG
GCTTGTGTGGAGGCCCCCAAGGGAAACCCCATCTGCAGCCTTCATGATCAGGGCGCTGGT
GGCAATGGCAATGTCCTAAAAGAGCTGAGTGACCCAGCTGGAGCCATCATTTACACCAGC
CGCTTCCAGCTTGGGGACCCAACCCTGAATGCCCTGGAAATCTGGGGGGCTGAGTACCAG
GAATCAAATGCTCTTCTGCTGAGGTCCCCCAACCGGGACTTCCTGACTCATGTCAGTGCC
CGTGAACGTTGCCCGGCTTGCTTCGTGGGCACCATCACTGGAGACCGGAGAATAGTGCTG
GTGGACGATCGGGAGTGTCCTGTCAGAAGAAATGGCCAGGGGGATGCCCCCCCGACACCC
CTGCCAACCCCTGTGGACCTGGAGCTCGGATGGGTGCTGGGCAAGATGCCTCGGAAGGAG
TTCTTCCTGCAGAGGAAGCCCCCCATGCTGCAGCCTCTGGCCTTGCCCCCAGGGCTGAGC
GTGCACCAGGCTCTGGAGAGGGTTCTGAGGCTGCCCGCCGTGGCCAGCAAGCGCTACCTC
ACCAATAAGGTGGACCGCTCTGTGGGAGGCCTGGTGGCCCAGCAGCAGTGCGTGGGGCCC
CTGCAAACTCCTCTGGCAGATGTAGCGGTTGTGGCACTGAGCCATGAGGAGCTCATAGGG
GCTGCCACAGCCTTGGGAGAACAGCCAGTCAAGAGCCTGCTGGACCCAAAAGTCGCCGCC
CGGCTGGCCGTGGCCGAAGCCCTCACCAACCTGGTGTTTGCTCTGGTCACTGACCTCCGG
GATGTGAAGTGTAGCGGGAACTGGATGTGGGCAGCCAAGCTCCCAGGGGAGGGCGCAGCT
TTGGCGGATGCCTGTGAGGCTATGGTGGCAGTGATGGCAGCCCTGGGTGTGGCAGTGGAT
GGTGGCAAGGACTCCCTCAGCATGGCTGCTCGGGTTGGCACTGAGACCGTGCGGGCTCCT
GGGTCACTGGTCATCTCAGCCTATGCCGTCTGCCCAGACATCACAGCCACTGTGACCCCA
GACCTCAAGCATCCTGAAGGGAGAGGCCATCTGCTCTATGTGGCTCTGAGCCCTGGGCAG
CACCGGCTCGGGGGCACAGCTCTGGCCCAGTGCTTCTCCCAGCTTGGGGAACACCCTCCA
GACCTGGACCTTCCTGAGAACTTGGTGCGGGCCTTCAGCATCACTCAGGGGCTGCTGAAA
GACCGCCTCCTCTGCTCAGGCCACGATGTCAGTGACGGAGGCCTCGTCACATGCCTGCTG
GAGATGGCCTTTGCTGGAAATTGCGGGCTACAGGTGGATGTGCCTGTCCCCAGGGTTGAT
GTCCTGTCTGTGCTGTTCGCTGAGGAGCCAGGCCTCGTGCTGGAGGTGCAGGAGCCAGAC
CTGGCCCAGGTGCTGAAGCGTTACCGGGATGCTGGCCTCCATTGCCTGGAGCTGGGCCAC
ACAGGCGAGGCCGGGCCCCACGCCATGGTCCGGGTGTCAGTGAACGGGGCTGTGGTTCTG
GAGGAGCCTGTTGGGGAGCTGCGAGCCCTCTGGGAGGAGACGAGTTTCCAGCTGGACCGG
CTACAGGCAGAGCCTCGCTGTGTGGCAGAGGAGGAACGGGGCCTGAGGGAGCGGATGGGG
CCCAGCTATTGCCTGCCCCCCACCTTTCCCAAAGCCTCCGTGCCCCGTGAGCCTGGTGGT
CCCAGCCCCCGAGTCGCCATCTTGCGAGAGGAGGGCAGTAATGGAGACCGGGAGATGGCC
GATGCCTTCCACTTAGCTGGGTTTGAGGTATGGGACGTGACCATGCAGGACCTCTGCTCT
GGGGCAATTGGGCTGGACACTTTCCGTGGCGTGGCCTTCGTGGGCGGCTTCAGCTATGCA
GATGTCCTGGGCTCTGCCAAAGGGTGGGCAGCTGCTGTGACCTTTCATCCCAGGGCTGGG
GCTGAGCTGAGGCGCTTCCGGAAGCGGCCAGACACCTTCAGCCTGGGCGTGTGTAATGGC
TGTCAACTGCTGGCTCTGCTCGGCTGGGTGGGAGGCGACCCCAATGAGGATGCTGCAGAG
ATGGGCCCTGACTCCCAGCCAGCCCGGCCAGGCCTTCTGCTACACCACAACCTGTCTGGG
CGCTACGAGTCTCGCTGGGCCAGCGTGCGTGTGGGGCCTGGGCCAGCCCTGATGCTGCGA
GGGATGGAGGGCGCCGTGCTGCCCGTGTGGAGTGCGCACGGGGAAGGTTACGTAGCATTT
TCTTCTCCGGAACTCCAAGCTCAGATTGAGGCCAGGGGCTTGGCTCCACTGCACTGGGCT
GATGATGACGGGAACCCCACAGAGCAGTACCCTCTGAATCCCAATGGGTCCCCAGGGGGC
GTGGCTGGCATCTGCTCCTGTGATGGCCGCCACCTGGCTGTCATGCCTCACCCTGAGCGG
GCCGTTAGGCCTTGGCAGTGGGCATGGCGACCCCCTCCATTTGATACTCTGACCACCTCC
CCCTGGCTCCAGCTCTTTATCAATGCCCGAAACTGGACCCTGGAAGGGAGCTGCTGA
Enzyme 30 GenBank Gene ID AK292804 Link Image
Enzyme 30 GeneCard ID A8K9T9 Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs Not Available
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 15228
Enzyme 31 Name cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K (Cysteine conjugate-beta lyase
Enzyme 31 Synonyms
  1. cytoplasmic (Glutamine transaminase K, kyneurenine aminotransferase), isoform CRA_a)
Enzyme 31 Gene Name CCBL1
Enzyme 31 Protein Sequence >cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K (Cysteine conjugate-beta lyase 
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
Enzyme 31 Number of Residues 422
Enzyme 31 Molecular Weight 47876
Enzyme 31 Theoretical pI 6.45
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Amino acid transport and metabolism
Enzyme 31 Specific Function Not Available
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function Not Available
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 158255792 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID A8K563 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name A8K563_HUMAN Link Image
Enzyme 31 PDB ID 1W7N Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1269 bp 
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTTATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
Enzyme 31 GenBank Gene ID AK291178 Link Image
Enzyme 31 GeneCard ID A8K563 Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID Not Available
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References Not Available
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 16463
Enzyme 32 Name cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
Enzyme 32 Synonyms
  1. SubName: cDNA FLJ43358 fis, clone NT2RP7014005, highly similar to CTP synthase 2 (EC 6.3.4.2)
  2. SubName: CTP synthase II, isoform CRA_a
Enzyme 32 Gene Name CTPS2
Enzyme 32 Protein Sequence >cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2) 
MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFV
LNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDA
VQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHV
SLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ
VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICS
IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQK
LCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDAD
STEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH
RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPY
LGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS
Enzyme 32 Number of Residues 586
Enzyme 32 Molecular Weight 65678
Enzyme 32 Theoretical pI 6.91
Enzyme 32 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
—
Enzyme 32 General Function Nucleotide transport and metabolism
Enzyme 32 Specific Function Not Available
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571] ALL_REAC R00571
  • (other) R00573
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID B3KWM2 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name B3KWM2_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID AK125332 Link Image
Enzyme 32 GeneCard ID B3KWM2 Link Image
Enzyme 32 GenAtlas ID Not Available
Enzyme 32 HGNC ID Not Available
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References Not Available
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 16912
Enzyme 33 Name Glutamyl-tRNA(Gln) amidotransferase subunit A homolog
Enzyme 33 Synonyms
  1. Glutaminyl-tRNA synthase-like protein 1
Enzyme 33 Gene Name QRSL1
Enzyme 33 Protein Sequence >Glutamyl-tRNA(Gln) amidotransferase subunit A homolog 
MLGRSLREVSAALKQGQITPTELCQKCLSLIKKTKFLNAYITVSEEVALKQAEESEKRYK
NGQSLGDLDGIPIAVKDNFSTSGIETTCASNMLKGYIPPYNATVVQKLLDQGALLMGKTN
LDEFAMGSGSTDGVFGPVKNPWSYSKQYREKRKQNPHSENEDSDWLITGGSSGGSAAAVS
AFTCYAALGSDTGGSTRNPAAHCGLVGFKPSYGLVSRHGLIPLVNSMDVPGILTRCVDDA
AIVLGALAGPDPRDSTTVHEPINKPFMLPSLADVSKLCIGIPKEYLVPELSSEVQSLWSK
AADLFESEGAKVIEVSLPHTSYSIVCYHVLCTSEVASNMARFDGLQYGHRCDIDVSTEAM
YAATRREGFNDVVRGRILSGNFFLLKENYENYFVKAQKVRRLIANDFVNAFNSGVDVLLT
PTTLSEAVPYLEFIKEDNRTRSAQDDIFTQAVNMAGLPAVSIPVALSNQGLPIGLQFIGR
AFCDQQLLTVAKWFEKQVQFPVIQLQELMDDCSAVLENEKLASVSLKQ
Enzyme 33 Number of Residues 528
Enzyme 33 Molecular Weight 57461
Enzyme 33 Theoretical pI 5.37
Enzyme 33 GO Classification
Function
  • amidase activity
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • glutamyl-tRNA(Gln) amidotransferase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein biosynthesis
Component
—
Enzyme 33 General Function Translation, ribosomal structure and biogenesis
Enzyme 33 Specific Function ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein Not Available
Enzyme 33 UniProtKB/Swiss-Prot ID Q9H0R6 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name QRSL1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence Not Available
Enzyme 33 GenBank Gene ID AL136679 Link Image
Enzyme 33 GeneCard ID Q9H0R6 Link Image
Enzyme 33 GenAtlas ID QRSL1 Link Image
Enzyme 33 HGNC ID HGNC:21020 Link Image
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available