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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Alanine (HMDB00161)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-05-21 14:58:04
Accession Number HMDB00161
Secondary Accession Numbers Not Available
Common Name L-Alanine
Description Alanine is a nonessential amino acid made in the body from the conversion of the carbohydrate pyruvate or the breakdown of DNA and the dipeptides carnosine and anserine. It is highly concentrated in muscle and is one of the most important amino acids released by muscle, functioning as a major energy source. Plasma alanine is often decreased when the BCAA (Branched Chain Amino Acids) are deficient. This finding may relate to muscle metabolism. Alanine is highly concentrated in meat products and other high-protein foods like wheat germ and cottage cheese. Alanine is an important participant as well as regulator in glucose metabolism. Alanine levels parallel blood sugar levels in both diabetes and hypoglycemia, and alanine reduces both severe hypoglycemia and the ketosis of diabetes. It is an important amino acid for lymphocyte reproduction and immunity. Alanine therapy has helped dissolve kidney stones in experimental animals. Normal alanine metabolism, like that of other amino acids, is highly dependent upon enzymes that contain vitamin B6. Alanine, like GABA, taurine and glycine, is an inhibitory neurotransmitter in the brain. http://www.dcnutrition.com/AminoAcids/)
Synonyms
  1. (2S)-2-Aminopropanoate
  2. (2S)-2-Aminopropanoic acid
  3. (S)-(+)-Alanine
  4. (S)-2-Aminopropanoate
  5. (S)-2-Aminopropanoic acid
  6. (S)-2-amino-Propanoate
  7. (S)-2-amino-Propanoic acid
  8. (S)-Alanine
  9. 2-Aminopropanoate
  10. 2-Aminopropanoic acid
  11. 2-Aminopropionate
  12. 2-Aminopropionic acid
  13. 2-Ammoniopropanoate
  14. Ala
  15. Alanine
  16. L-(+)-Alanine
  17. L-2-Aminopropanoate
  18. L-2-Aminopropanoic acid
  19. L-2-Aminopropionate
  20. L-2-Aminopropionic acid
  21. L-a-Alanine
  22. L-a-Aminopropionate
  23. L-a-Aminopropionic acid
  24. a-Alanine
  25. a-Aminopropionate
  26. a-Aminopropionic acid
  27. alpha-Aminopropanoate
  28. alpha-Aminopropanoic acid
  29. L-alpha-Alanine
  30. L-alpha-Aminopropionate
  31. L-alpha-Aminopropionic acid
  32. alpha-Alanine
  33. alpha-Aminopropionate
  34. alpha-Aminopropionic acid
  35. 2-Ammoniopropanoic acid
Chemical IUPAC Name (2S)-2-aminopropanoic acid
Chemical Formula C3H7NO2
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
  • alpha-aminoacid
Biofunction
  • Component of Alanine and aspartate metabolism
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Glutamate metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Tryptophan metabolism
Application
Source
  • Endogenous
Average Molecular Weight 89.093
Monoisotopic Molecular Weight 89.047676
Isomeric SMILES C[C@H](N)C(O)=O
Canonical SMILES CC(N)C(O)=O
KEGG Compound ID C00041 Link Image
BioCyc ID L-ALPHA-ALANINE Link Image
BiGG ID 33629 Link Image
Wikipedia Link 2-Aminopropanoic acid Link Image
NuGOwiki Link HMDB00161 Link Image
Metagene Link HMDB00161 Link Image
METLIN ID Not Available
PubChem Compound 5950 Link Image
PubChem Substance 700553 Link Image
ChEBI ID 16977 Link Image
CAS Registry Number 56-41-7
InChI Identifier InChI=1/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1
Synthesis Reference Chibata I; Kakimoto T; Kato J Enzymatic production of L-alanine by Pseudomonas dacunhae. Applied microbiology (1965), 13(5), 638-45.
Melting Point (Experimental) 300 oC
Experimental Water Solubility 164.0 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 204 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 446.99997 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -2.85 [SANGSTER (1994)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.05 [Predicted by ALOGPS]; -2.8 [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 1KL6 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
  • Extracellular
  • lysosome
  • mitochondria
  • peroxisome
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 333.0 (259.0-407.0) 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 375.0 +/- 50.0 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 369.0 +/- 88.0 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 585.0 +/- 22.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid Blood
Value 291.00 (143.00-439.00) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid CSF
Value 23.2 +/- 5.1 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 27.0 (10.0-44.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
Biofluid CSF
Value 37.8 +/- 6.8 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 30.8 +/- 8.7 uM
Age Adult:>18 yrs old
Sex N/A
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 26.3 +/- 7.4 uM
Age Adult:>18 yrs old
Sex N/A
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 46 +/- 27 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 13.2 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
Biofluid Urine
Value 2.0 (1.0-3.5) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 12.3 +/- 5.6 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 22.0 +/- 11.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 22.0 +/- 10.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 33.5 +/- 14.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Psihogios NG, Gazi IF, Elisaf MS, Seferiadis KI, Bairaktari ET: Gender-related and age-related urinalysis of healthy subjects by NMR-based metabonomics. NMR Biomed. 2008 Mar;21(3):195-207. [PubMed Link Image]
Biofluid Urine
Value 34.3 +/- 11.5 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Psihogios NG, Gazi IF, Elisaf MS, Seferiadis KI, Bairaktari ET: Gender-related and age-related urinalysis of healthy subjects by NMR-based metabonomics. NMR Biomed. 2008 Mar;21(3):195-207. [PubMed Link Image]
Biofluid Urine
Value 4.23 +/- 0.64 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Urine
Value 113.35 +/- 69.81 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 39.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
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]
Biofluid Urine
Value 271 +/- 10 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 274.0 (250.0-298.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Dengue fever
Comments Not Available
References
  • Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [PubMed Link Image]
Biofluid Blood
Value 296.0 (277.0-316.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Acute seizures Ethanolaminosis: increased
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 589.0 +/- 15.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Heart failure
Comments Non-diabetic patients with chronic heart failure
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid Blood
Value 1000.00 (800.00-1200.00) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid CSF
Value 0.16 (0.13-0.18) uM
Age Adult:>18 yrs old
Sex Both
Condition Meningitis
Comments Bacterial
References
  • Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
Biofluid CSF
Value 19.2 (16.1-22.3) uM
Age Adult:>18 yrs old
Sex Both
Condition Tuberculosis
Comments Not Available
References
  • Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
Biofluid CSF
Value 46.1 +/- 13.5 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 34.8 +/- 7.8 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 4.04 +/- 0.57 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Urine
Value 76.3 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Paraquat poisoning
Comments Not Available
References
  • Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
Biofluid Urine
Value 23 (10-55) umol/mmol creatinine
Age N/A
Sex Both
Condition Lung Cancer
Comments Not Available
References
  • HMP experimental
Associated Disorders
Condition References
Dengue fever
  • Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [PubMed Link Image]
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]
Heart failure
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [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]
Lung Cancer
  • HMP experimental
Meningitis
  • Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
Paraquat poisoning
  • Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
Schizophrenia
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Tuberculosis
  • Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Alanine Metabolism SMP00055 Link Image map00250 Link Image
Glucose-Alanine Cycle SMP00127 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Selenoamino Acid Metabolism SMP00029 Link Image map00450 Link Image
Transcription/Translation SMP00019 Link Image
Urea Cycle SMP00059 Link Image map00330 Link Image
General References
  1. Iioka H, Hisanaga H, Moriyama IS, Akada S, Shimamoto T, Yamada Y, Ichijo M: Characterization of human placental activity for transport of L-alanine, using brush border (microvillous) membrane vesicles. Placenta. 1992 Mar-Apr;13(2):179-90. [PubMed Link Image]
  2. 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]
  3. 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]
  4. 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]
  5. Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
  6. Saklatvala J: Hydrolysis of the elastase substrate succinyltrialanine nitroanilide by a metal-dependent enzyme in rheumatoid synovial fluid. J Clin Invest. 1977 May;59(5):794-801. [PubMed Link Image]
  7. Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
  8. 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]
  9. Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [PubMed Link Image]
  10. Stahl A, Frick A, Imler M, Schlienger JL: Semiautomated enzymic microassay for plasma L-alanine. Enzyme. 1979;24(5):294-301. [PubMed Link Image]
  11. 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]
  12. 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]
  13. Wikipedia Link Image
Metabolic Enzymes
  1. Kynureninase
  2. Alanine--glyoxylate aminotransferase 2, mitochondrial precursor
  3. Alanyl-tRNA synthetase, cytoplasmic
  4. Serine--pyruvate aminotransferase
  5. Alanine aminotransferase 1
  6. Peptidoglycan recognition protein precursor
  7. Large neutral amino acids transporter small subunit 2
  8. Cysteine desulfurase, mitochondrial precursor
  9. System N amino acid transporter 1
  10. Neutral amino acid transporter A
  11. Alanine aminotransferase 2
  12. Selenocysteine lyase
  13. Alanine aminotransferase
  14. Kynureninase
  15. Alanine--glyoxylate aminotransferase 2-like 2
  16. cDNA FLJ77866, highly similar to Homo sapiens peptidoglycan recognition protein L (PGLYRP) mRNA (Peptidoglycan recognition protein 2, isoform CRA_a)
  17. Peptidoglycan recognition protein I-alpha
  18. Peptidoglycan recognition protein 4 (PGLYRP4 protein)
  19. cDNA FLJ10608 fis, clone NT2RP2005239, highly similar to Cysteine desulfurase, mitochondrial (EC 2.8.1.7)
  20. Probable alanyl-tRNA synthetase, mitochondrial
Enzyme 1 [top]
Enzyme 1 ID 5561
Enzyme 1 Name Kynureninase
Enzyme 1 Synonyms
  1. L-kynurenine hydrolase
Enzyme 1 Gene Name KYNU
Enzyme 1 Protein Sequence >Kynureninase
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKK
SVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEK
RGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN
Enzyme 1 Number of Residues 465
Enzyme 1 Molecular Weight 52352
Enzyme 1 Theoretical pI 7.04
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
  • kynureninase activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
  • NAD biosynthesis
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • indolalkylamine metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
  • tryptophan catabolism
  • tryptophan metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic (AA) and 3- hydroxyanthranilic acids (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-kynurenine + H2O = anthranilate + L-alanine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1323715 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16719 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name KYNU_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1398 bp
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCATTAGTGGGATGGTTTGGCCATGAACTCAGCACCAGATTTAAGATGGATAACAAACTG
CAGTTAATCCCTGGGGTCTGTGGATTCCGAATTTCAAATCCTCCCATTTTGTTGGTCTGT
TCCTTGCATGCTAGTTTAGAGATCTTTAAGCAAGCGACAATGAAGGCATTGCGGAAAAAA
TCTGTTTTGCTAACTGGCTATCTGGAATACCTGATCAAGCATAACTATGGCAAAGATAAA
GCAGCAACCAAGAAACCAGTTGTGAACATAATTACTCCGTCTCATGTAGAGGAGCGGGGG
TGCCAGCTAACAATAACATTTTCTGTTCCAAACAAAGATGTTTTCCAAGAACTAGAAAAA
AGAGGAGTGGTTTGTGACAAGCGGAATCCAAATGGCATTCGAGTGGCTCCAGTTCCTCTC
TATAATTCTTTCCATGATGTTTATAAATTTACCAATCTGCTCACTTCTATACTTGACTCT
GCAGAAACAAAAAATTAG
Enzyme 1 GenBank Gene ID U57721 Link Image
Enzyme 1 GeneCard ID KYNU Link Image
Enzyme 1 GenAtlas ID KYNU Link Image
Enzyme 1 HGNC ID HGNC:6469 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q22.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Alberati-Giani D, Buchli R, Malherbe P, Broger C, Lang G, Kohler C, Lahm HW, Cesura AM: Isolation and expression of a cDNA clone encoding human kynureninase. Eur J Biochem. 1996 Jul 15;239(2):460-8. [PubMed Link Image]
  2. Toma S, Nakamura M, Tone S, Okuno E, Kido R, Breton J, Avanzi N, Cozzi L, Speciale C, Mostardini M, Gatti S, Benatti L: Cloning and recombinant expression of rat and human kynureninase. FEBS Lett. 1997 May 12;408(1):5-10. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5633
Enzyme 2 Name Alanine--glyoxylate aminotransferase 2, mitochondrial precursor
Enzyme 2 Synonyms
  1. (R-3-amino-2-methylpropionate--pyruvate transaminase
  2. AGT 2
  3. Beta-alanine-pyruvate aminotransferase
  4. Beta- ALAAT II
  5. D-AIBAT
Enzyme 2 Gene Name AGXT2
Enzyme 2 Protein Sequence >Alanine--glyoxylate aminotransferase 2, mitochondrial precursor
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
Enzyme 2 Number of Residues 514
Enzyme 2 Molecular Weight 57157
Enzyme 2 Theoretical pI 7.91
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
Component
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function L-alanine + glyoxylate = pyruvate + glycine
Enzyme 2 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 2 Reactions
  • L-alanine + glyoxylate = pyruvate + glycine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-24
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12406973 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BYV1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AGT2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1545 bp
ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGCAGACAGGATTTGGAAGGTTGGGCTCTCACTTCTGGGGCTTCCAAACCCACGAT
GTCCTGCCTGACATTGTCACCATGGCTAAAGGGATTGGGAATGGCTTTCCCATGGCAGCA
GTCATAACCACTCCAGAGATTGCCAAATCTTTGGCGAAATGCCTGCAGCACTTCAACACC
TTTGGAGGGAACCCCATGGCCTGTGCCATTGGATCTGCTGTGCTTGAGGTGATTAAAGAA
GAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTACTAAAGTTTGCTAAG
CTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGTCTCATGATAGGCATA
GAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAAGAAGTAAATCAGATC
CATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGCATTTTTTCTCAGACA
TTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGATTTTGCAGTAGAAGTA
TTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
Enzyme 2 GenBank Gene ID AJ292204 Link Image
Enzyme 2 GeneCard ID AGXT2 Link Image
Enzyme 2 GenAtlas ID AGXT2 Link Image
Enzyme 2 HGNC ID HGNC:14412 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5897
Enzyme 3 Name Alanyl-tRNA synthetase, cytoplasmic
Enzyme 3 Synonyms
  1. Alanine--tRNA ligase
  2. AlaRS
  3. Renal carcinoma antigen NY-REN-42
Enzyme 3 Gene Name AARS
Enzyme 3 Protein Sequence >Alanyl-tRNA synthetase, cytoplasmic
MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPS
HPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALE
LLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGD
TGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDT
GMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLAD
HARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDA
FPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGF
PVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEV
TDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGG
QIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRP
IMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMI
EAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSV
EFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAK
VKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKR
VLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKIT
CLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQ
LRLGDVKN
Enzyme 3 Number of Residues 968
Enzyme 3 Molecular Weight 106812
Enzyme 3 Theoretical pI 5.18
Enzyme 3 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • alanine-tRNA ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleic acid binding
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • alanyl-tRNA aminoacylation
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
Enzyme 3 General Function Translation, ribosomal structure and biogenesis
Enzyme 3 Specific Function ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1015321 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P49588 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SYAC_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2907 bp
ATGGACTCTACTCTAACAGCAAGTGAAATCCGGCAGCGATTTATAGATTTCTTCAAGAGG
AACGAGCATACGTATGTTCACTCGTCTGCCACCATCCCATTGGATGACCCCACTTTGCTC
TTTGCCAATGCAGGCATGAACCAGTTTAAACCCATTTTCCTGAACACAATTGACCCATCT
CACCCCATGGCAAAGCTGAGCAGAGCTGCCAATACCCAGAAGTGCATCCGGGCTGGGGGC
AAACAAAATGACCTGGACGATGTGGGCAAGGATGTCTATCATCACACCTTCTTCGAGATG
CTGGGCTCTTGGTCTTTTGGAGATTACTTTAAGGAATTGGCATGTAAGATGGCTCTGGAA
CTCCTCACCCAAGAGTTTGGCATTCCCATTGAAAGACTTTATGTTACTTACTTTGGCGGG
GATGAAGCAGCTGGCTTAGAAGCAGATCTGGAATGCAAACAGATCTGGCAAAATTTGGGG
CTGGATGACACCAAAATCCTCCCAGGCAACATGAAGGATAACTTCTGGGAGATGGGTGAC
ACGGGCCCCTGTGGTCCTTGCAGTGAGATCCACTACGACCGGATTGGTGGTCGGGACGCC
GCACATCTTGTCAACCAGGACGACCCTAATGTGCTGGAGATCTGGAACCTTGTGTTCATC
CAGTATAACAGGGAAGCTGATGGCATTCTGAAACCTCTTCCCAAGAAAAGCATTGACACA
GGGATGGGCCTGGAACGACTGGTATCTGTGCTGCAGAATAAGATGTCCAACTATGACACT
GACCTTTTTGTCCCTTACTTTGAAGCCATTCAGAAGGGCACAGGTGCCCGACCATACACT
GGGAAAGTTGGTGCTGAGGATGCCGATGGGATTGACATGGCCTACCGGGTGCTGGCTGAC
CATGCTCGGACCATCACTGTGGCACTGGCTGATGGTGGCCGGCCTGACAACACAGGGCGT
GGATATGTGTTGAGACGGATTCTCCGCCGAGCTGTCCGATACGCCCATGAAAAGCTCAAT
GCCAGCAGGGGCTTCTTTGCTACGTTAGTGGATGTTGTCGTCCAGTCCCTGGGAGATGCA
TTTCCTGAGCTGAAGAAGGACCCAGACATGGTGAAGGACATCATTAATGAAGAAGAGGTG
CAGTTTCTCAAGACTCTCAGCAGAGGGCGTCGCATCCTGGACAGGAAAATTCAGAGCCTG
GGAGACAGCAAGACCATTCCCGGAGACACTGCTTGGCTCCTCTATGACACCTATGGGTTT
CCAGTGGATCTGACTGGACTGATTGCTGAAGAGAAGGGCCTGGTGGTAGACATGGATGGC
TTTGAAGAGGAGAGGAAACTGGCCCAGCTGAAATCACAGGGCAAGGGAGCTGGTGGGGAA
GACCTCATTATGCTGGACATTTACGCTATCGAAGAGCTCCGGGCACGGGGTCTGGAGGTC
ACAGATGATTCCCCAAAGTACAATTACCATTTGGACTCCAGTGGTAGCTATGTATTTGAG
AACACAGTGGCTACGGTGATGGCTCTGCGCAGGGAGAAGATGTTCGTGGAAGAGGTGTCC
ACAGGCCAGGAGTGTGGAGTGGTGCTGGACAAGACCTGTTTCTATGCTGAGCAAGGAGGC
CAGATCTATGACGAAGGCTACCTGGTGAAGGTGGATGACAGCAGTGAAGATAAAACAGAG
TTTACAGTGAAGAATGCTCAGGTCCGAGGAGGGTATGTGCTACACATTGGAACCATCTAC
GGTGACCTGAAAGTGGGGGATCAGGTCTGGCTGTTTATTGATGAGCCCCGACGAAGACCC
ATCATGAGCAACCACACAGCTACGCACATTCTGAACTTCGCCCTGCGCTCAGTGCTTGGG
GAAGCTGACCAGAAAGGCTCATTGGTTGCTCCTGACCGCCTCAGATTTGACTTTACTGCC
AAGGGAGCCATGTCCACCCAACAGATCAAGAAGGCTGAAGAGATTGCTAATGAGATGATT
GAGGCAGCCAAGGCCGTCTATACCCAGGATTGCCCCCTGGCAGCAGCGAAAGCCATCCAG
GGCCTACGGGCTGTGTTTGATGAGACCTATCCTGACCCTGTGCGAGTCGTCTCCATTGGG
GTCCCGGTGTCCGAGTTGCTGGATGACCCCTCTGGGCCTGCTGGCTCCCTGACTTCTGTT
GAGTTCTGTGGGGGAACGCACCTGCGGAACTCGAGTCATGCAGGAGCTTTTGTGATCGTG
ACGGAAGAAGCCATTGCCAAGGGTATCCGGAGGATTGTGGCTGTCACAGGTGCCGAGGCC
CAGAAGGCCCTCAGGAAAGCAGAGAGCTTGAAGAAATGTCTCTCTGTCATGGAAGCCAAA
GTGAAGGCTCAGACTGCTCCAAACAAGGATGTGCAGAGGGAGATCGCTGACCTTGGAGAG
GCCCTGGCCACTGCAGTCATCCCCCAGTGGCAGAAGGATGAATTGCGGGAGACTCTCAAA
TCCCTAAAGAAGGTCATGGATGACTTGGACCGAGCCAGCAAAGCCGATGTCCAGAAACGA
GTGTTAGAGAAGACGAAGCAGTTCATCGACAGCAACCCCAACCAGCCTCTTGTCATCCTG
GAGATGGAGAGCGGCGCCTCAGCCAAGGCCCTGAATGAAGCCTTGAAGCTCTTCAAGATG
CACTCCCCTCAGACTTCTGCCATGCTCTTCACGGTGGACAATGAGGCTGGCAAGATCACG
TGCCTGTGTCAAGTCCCCCAGAATGCAGCCAATCGGGGCTTAAAAGCCAGCGAGTGGGTG
CAGCAGGTGTCAGGCTTGATGGACGGTAAAGGTGGTGGCAAGGATGTGTCTGCACAGGCC
ACAGGCAAGAACGTTGGCTGCCTGCAGGAGGCGCTGCAGCTGGCCACTTCCTTCGCCCAG
CTGCGCCTCGGGGATGTAAAGAACTGA
Enzyme 3 GenBank Gene ID D32050 Link Image
Enzyme 3 GeneCard ID AARS Link Image
Enzyme 3 GenAtlas ID AARS Link Image
Enzyme 3 HGNC ID HGNC:20 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Shiba K, Ripmaster T, Suzuki N, Nichols R, Plotz P, Noda T, Schimmel P: Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition. Biochemistry. 1995 Aug 22;34(33):10340-9. [PubMed Link Image]
  2. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6069
Enzyme 4 Name Serine--pyruvate aminotransferase
Enzyme 4 Synonyms
  1. SPT
  2. Alanine-- glyoxylate aminotransferase
  3. AGT
Enzyme 4 Gene Name AGXT
Enzyme 4 Protein Sequence >Serine--pyruvate aminotransferase
MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL
Enzyme 4 Number of Residues 392
Enzyme 4 Molecular Weight 43011
Enzyme 4 Theoretical pI 8.55
Enzyme 4 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function L-serine + pyruvate = 3-hydroxypyruvate + L- alanine
Enzyme 4 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 4 Reactions
  • L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 36582 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P21549 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SPYA_HUMAN Link Image
Enzyme 4 PDB ID 1H0C Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1179 bp
ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA
Enzyme 4 GenBank Gene ID X56092 Link Image
Enzyme 4 GeneCard ID AGXT Link Image
Enzyme 4 GenAtlas ID AGXT Link Image
Enzyme 4 HGNC ID HGNC:341 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 2q36-q37
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed Link Image]
  2. Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed Link Image]
  3. Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed Link Image]
  4. Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed Link Image]
  5. Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed Link Image]
  6. Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed Link Image]
  7. Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed Link Image]
  8. Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed Link Image]
  9. Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed Link Image]
  10. von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed Link Image]
  11. Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed Link Image]
  12. Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6131
Enzyme 5 Name Alanine aminotransferase 1
Enzyme 5 Synonyms
  1. ALT1
  2. Glutamic--pyruvic transaminase 1
  3. GPT 1
  4. Glutamic--alanine transaminase 1
Enzyme 5 Gene Name GPT
Enzyme 5 Protein Sequence >Alanine aminotransferase 1
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
Enzyme 5 Number of Residues 496
Enzyme 5 Molecular Weight 54638
Enzyme 5 Theoretical pI 7.20
Enzyme 5 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 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles
Enzyme 5 Pathways
Enzyme 5 Reactions
  • L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1763096 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P24298 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ALAT1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1491 bp
ATGGCCTCGAGCACAGGTGACCGGAGCCAGGCGGTGAGGCATGGACTGAGGGCGAAGGTG
CTGACGCTGGACGGCATGAACCCGCGTGTGCGGAGAGTGGAGTACGCAGTGCGTGGCCCC
ATAGTGCAGCGAGCCTTGGAGCTGGAGCAGGAGCTGCGCCAGGGTGTGAAGAAGCCTTTC
ACCGAGGTCATCCGTGCCAACATCGGGGACGCACAGGCTATGGGGCAGAGGCCCATCACC
TTCCTGCGCCAGGTCTTGGCCCTCTGTGTTAACCCTGATCTTCTGAGCAGCCCCAACTTC
CCTGACGATGCCAAGAAAAGGGCGGAGCGCATCTTGCAGGCGTGTGGGGGCCACAGTCTG
GGGGCCTACAGCGTCAGCTCCGGCATCCAGCTGATCCGGGAGGACGTGGCGCGGTACATT
GAGAGGCGTGACGGAGGCATCCCTGCGGACCCCAACAACGTCTTCCTGTCCACAGGGGCC
AGCGATGCCATCGTGACGGTGCTGAAGCTGCTGGTGGCCGGCGAGGGCCACACACGCACG
GGTGTGCTCATCCCCATCCCCCAGTACCCACTCTACTCGGCCACGCTGGCAGAGCTGGGC
GCAGTGCAGGTGGATTACTACCTGGACGAGGAGCGTGCCTGGGCGCTGGACGTGGCCGAG
CTTCACCGTGCACTGGGCCAGGCGCGTGACCACTGCCGCCCTCGTGCGCTCTGTGTCATC
AACCCTGGCAACCCCACCGGGCAGGTGCAGACCCGCGAGTGCATCGAGGCCGTGATCCGC
TTCGCCTTCGAAGAGCGGCTCTTTCTGCTGGCGGACGAGGTGTACCAGGACAACGTGTAC
GCCGCGGGTTCGCAGTTCCACTCATTCAAGAAGGTGCTCATGGAGATGGGGCCGCCCTAC
GCCGGGCAGCAGGAGCTTGCCTCCTTCCACTCCACCTCCAAGGGCTACATGGGCGAGTGC
GGGTTCCGCGGCGGCTATGTGGAGGTGGTGAACATGGACGCTGCAGTGCAGCAGCAGATG
CTGAAGCTGATGAGTGTGCGGCTGTGCCCGCCGGTGCCAGGACAGGCCCTGCTGGACCTG
GTGGTCAGCCCGCCCGCGCCCACCGACCCCTCCTTTGCGCAGTTCCAGGCTGAGAAGCAG
GCAGTGCTGGCAGAGCTGGCGGCCAAGGCCAAGCTCACCGAGCAGGTCTTCAATGAGGCT
CCTGGCATCAGCTGCAACCCAGTGCAGGGCGCCATGTACTCCTTCCCGCGCGTGCAGCTG
CCCCCGCGGGCGGTGGAGCGCGCTCAGGAGCTGGGCCTGGCCCCCGATATGTTCTTCTGC
CTGCGCCTCCTGGAGGAGACCGGCATCTGCGTGGTGCCAGGGAGCGGCTTTGGGCAGCGG
GAAGGCACCTACCACTTCCGGATGACCATTCTGCCCCCCTTGGAGAAACTGCGGCTGCTG
CTGGAGAAGCTGAGCAGGTTCCATGCCAAGTTCACCCTCGAGTACTCCTGA
Enzyme 5 GenBank Gene ID U70732 Link Image
Enzyme 5 GeneCard ID GPT Link Image
Enzyme 5 GenAtlas ID GPT Link Image
Enzyme 5 HGNC ID HGNC:4552 Link Image
Enzyme 5 Chromosome Location 8
Enzyme 5 Locus 8q24.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Sohocki MM, Sullivan LS, Harrison WR, Sodergren EJ, Elder FF, Weinstock G, Tanase S, Daiger SP: Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites. Genomics. 1997 Mar 1;40(2):247-52. [PubMed Link Image]
  2. Ishiguro M, Takio K, Suzuki M, Oyama R, Matsuzawa T, Titani K: Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods. Biochemistry. 1991 Oct 29;30(43):10451-7. [PubMed Link Image]
  3. Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7528
Enzyme 6 Name Peptidoglycan recognition protein precursor
Enzyme 6 Synonyms
  1. PGRP-S
Enzyme 6 Gene Name PGLYRP1
Enzyme 6 Protein Sequence >Peptidoglycan recognition protein precursor
MSRRSMLLAWALPSLLRLGAAQETEDPACCSPIVPRNEWKALASECAQHLSLPLRYVVVS
HTAGSSCNTPASCQQQARNVQHYHMKTLGWCDVGYNFLIGEDGLVYEGRGWNFTGAHSGH
LWNPMSIGISFMGNYMDRVPTPQAIRAAQGLLACGVAQGALRSNYVLKGHRDVQRTLSPG
NQLYHLIQNWPHYRSP
Enzyme 6 Number of Residues 196
Enzyme 6 Molecular Weight 21731
Enzyme 6 Theoretical pI 8.68
Enzyme 6 GO Classification
Function
  • N-acetylmuramoyl-L-alanine amidase activity
  • binding
  • 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 linear amides
  • protein binding
Process
  • carbohydrate metabolism
  • cellular carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • peptidoglycan catabolism
  • peptidoglycan metabolism
  • physiological process
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Binds specifically to peptidoglycan and is involved in innate immunity
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-21
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 3342533 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O75594 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PGRP_HUMAN Link Image
Enzyme 6 PDB ID 1YCK Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >591 bp
ATGTCCCGCCGCTCTATGCTGCTTGCCTGGGCTCTTCCCAGCCTCCTTCGACTCGGAGCG
GCTCAGGAGACAGAAGACCCGGCCTGCTGCAGCCCCATAGTGCCCCGGAACGAGTGGAAG
GCCCTGGCATCAGAGTGCGCCCAGCACCTGAGCCTGCCCTTACGCTATGTGGTGGTATCG
CACACGGCGGGCAGCAGCTGCAACACCCCCGCCTCGTGCCAGCAGCAGGCCCGGAATGTG
CAGCACTACCACATGAAGACACTGGGCTGGTGCGACGTGGGCTACAACTTCCTGATTGGA
GAAGACGGGCTCGTATACGAGGGCCGTGGCTGGAACTTCACGGGTGCCCACTCAGGTCAC
TTATGGAACCCCATGTCCATTGGCATCAGCTTCATGGGCAACTACATGGATCGGGTGCCC
ACACCCCAGGCCATCCGGGCAGCCCAGGGTCTACTGGCCTGCGGTGTGGCTCAGGGAGCC
CTGAGGTCCAACTATGTGCTCAAAGGACACCGGGATGTGCAGCGTACACTCTCTCCAGGC
AACCAGCTCTACCACCTCATCCAGAATTGGCCACACTACCGCTCCCCCTGA
Enzyme 6 GenBank Gene ID AF076483 Link Image
Enzyme 6 GeneCard ID PGLYRP1 Link Image
Enzyme 6 GenAtlas ID PGLYRP1 Link Image
Enzyme 6 HGNC ID HGNC:8904 Link Image
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19q13.2-q13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kang D, Liu G, Lundstrom A, Gelius E, Steiner H: A peptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):10078-82. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Liu C, Xu Z, Gupta D, Dziarski R: Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. J Biol Chem. 2001 Sep 14;276(37):34686-94. Epub 2001 Jul 18. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7884
Enzyme 7 Name Large neutral amino acids transporter small subunit 2
Enzyme 7 Synonyms
  1. L-type amino acid transporter 2
  2. hLAT2
Enzyme 7 Gene Name SLC7A8
Enzyme 7 Protein Sequence >Large neutral amino acids transporter small subunit 2
MEEGARHRNNTEKKHPGGGESDASPEAGSGGGGVALKKEIGLVSACGIIVGNIIGSGIFV
SPKGVLENAGSVGLALIVWIVTGFITVVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGF
LRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSV
RWATRVQDIFTAGKLLALALIIIMGIVQICKGEYFWLEPKNAFENFQEPDIGLVALAFLQ
GSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYVTAMSPQELLASN
AVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVK
RCTPIPALLFTCISTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPI
KINLLFPIIYLLFWAFLLVFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFSDFI
ELLTLVSQKMCVVVYPEVERGSGTEEANEDMEEQQQPMYQPTPTKDKDVAGQPQP
Enzyme 7 Number of Residues 535
Enzyme 7 Molecular Weight 58382
Enzyme 7 Theoretical pI 5.75
Enzyme 7 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 7 General Function Amino acid transport and metabolism
Enzyme 7 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 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 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 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 6642960 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9UHI5 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name LAT2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID AF171669 Link Image
Enzyme 7 GeneCard ID SLC7A8 Link Image
Enzyme 7 GenAtlas ID SLC7A8 Link Image
Enzyme 7 HGNC ID HGNC:11066 Link Image
Enzyme 7 Chromosome Location 14
Enzyme 7 Locus 14q11.2
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8009
Enzyme 8 Name Cysteine desulfurase, mitochondrial precursor
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name NFS1
Enzyme 8 Protein Sequence >Cysteine desulfurase, mitochondrial precursor
MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
Enzyme 8 Number of Residues 457
Enzyme 8 Molecular Weight 50196
Enzyme 8 Theoretical pI 8.45
Enzyme 8 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-23
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 24042327 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9Y697 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NFS1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1374 bp
ATGCTGCTCCGAGTCGCTTGGAGGCGGGCGGCAGTGGCGGTGACAGCGGCTCCAGGGCCG
AAGCCCGCGGCGCCCACTCGGGGGCTGCGCCTGCGCGTTGGAGACCGTGCTCCTCAGTCT
GCGGTTCCCGCAGATACAACCGCTGCCCCGGAGGTGGGGCCAGTGCTGCGACCTCTCTAT
ATGGATGTGCAAGCTACAACTCCTCTGGACCCCCGGGTGCTTGATGCCATGCTCCCTTAC
CTAATCAACTACTATGGGAACCCACACTCCCGGACACATGCTTATGGCTGGGAGAGTGAG
GCAGCCATGGAACGTGCTCGTCAGCAAGTAGCATCTCTGATTGGAGCTGATCCTCGTGAG
ATCATTTTTACTAGTGGTGCTACTGAATCCAACAACATAGCAATTAAGGGGGTGGCCCGA
TTCTACAGGTCACGGAAAAAGCACTTGATCACCACCCAGACAGAACACAAATGTGTCTTG
GACTCCTGCCGTTCACTGGAAGCTGAGGGCTTTCAGGTCACCTACCTCCCAGTGCAGAAG
AGTGGGATCATTGACCTAAAGGAACTAGAGGCTGCTATCCAGCCAGATACTAGCCTGGTG
TCAGTCATGACTGTGAACAATGAGATTGGAGTGAAGCAGCCTATTGCAGAAATAGGGCGG
ATTTGCAGTTCCAGAAAGGTATATTTCCATACTGATGCAGCCCAGGCTGTTGGAAAAATC
CCACTTGATGTCAATGACATGAAAATTGATCTCATGAGCATTAGTGGTCACAAAATCTAC
GGTCCCAAAGGGGTTGGTGCCATCTACATCCGTCGCCGGCCCCGTGTGCGTGTGGAGGCC
CTGCAGAGTGGAGGGGGGCAGGAGCGGGGTATGCGGTCTGGGACAGTGCCCACACCCTTA
GTGGTGGGGTTGGGGGCTGCGTGTGAGGTGGCACAGCAAGAGATGGAGTATGACCACAAG
CGAATCTCAAAGTTGTCAGAGCGGCTGATACAGAATATAATGAAGAGCCTTCCAGATGTG
GTGATGAATGGGGACCCTAAGCACCATTATCCCGGCTGTATCAACCTCTCCTTTGCATAT
GTGGAAGGGGAAAGTCTGCTGATGGCACTGAAGGACGTTGCCTTATCCTCAGGGAGTGCC
TGCACCTCTGCATCCCTGGAGCCCTCTTATGTGCTTAGAGCAATTGGCACTGATGAGGAT
TTAGCGCACTCTTCTATCAGGTTTGGAATTGGCGCTTTCACTACAGAGGAGGAAGTGGAC
TACACAGTGGAGAAATGCATTCAGCATGTGAATCGTCTTCGAGAAATGAGCCCTCTCTGG
GAGATGGTTCAGGATGGCATTGACCTCAAGAGCATCAAGTGGACCCAACACTAG
Enzyme 8 GenBank Gene ID AF097025 Link Image
Enzyme 8 GeneCard ID NFS1 Link Image
Enzyme 8 GenAtlas ID NFS1 Link Image
Enzyme 8 HGNC ID HGNC:15910 Link Image
Enzyme 8 Chromosome Location 20
Enzyme 8 Locus 20q11.22
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Land T, Rouault TA: Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol Cell. 1998 Dec;2(6):807-15. [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]
  3. Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G: Characterization of 16 novel human genes showing high similarity to yeast sequences. Yeast. 2001 Jan 15;18(1):69-80. [PubMed Link Image]
  4. Tong WH, Rouault T: Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 2000 Nov 1;19(21):5692-700. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8562
Enzyme 9 Name System N amino acid transporter 1
Enzyme 9 Synonyms
  1. SN1
  2. N-system amino acid transporter 1
  3. Solute carrier family 38 member 3
Enzyme 9 Gene Name SLC38A3
Enzyme 9 Protein Sequence >System N amino acid transporter 1
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 9 Number of Residues 504
Enzyme 9 Molecular Weight 55774
Enzyme 9 Theoretical pI 8.01
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Amino acid transport and metabolism
Enzyme 9 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 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-111
Enzyme 9 Transmembrane Regions
  • 83-103 106-126 144-164 187-207 213-233 324-344 366-386 408-428 431-451 471-491
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID Q99624 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name S38A3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AF244548 Link Image
Enzyme 9 GeneCard ID SLC38A3 Link Image
Enzyme 9 GenAtlas ID SLC38A3 Link Image
Enzyme 9 HGNC ID HGNC:18044 Link Image
Enzyme 9 Chromosome Location 3
Enzyme 9 Locus 3p21.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 8650
Enzyme 10 Name Neutral amino acid transporter A
Enzyme 10 Synonyms
  1. SATT
  2. Solute carrier family 1 member 4
  3. Alanine/serine/cysteine/ threonine transporter
  4. ASCT1
Enzyme 10 Gene Name SLC1A4
Enzyme 10 Protein Sequence >Neutral amino acid transporter A
MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGA
ALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAY
FGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFP
SNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKL
GSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFA
SILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENN
GVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGA
AGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQK
ATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL
Enzyme 10 Number of Residues 532
Enzyme 10 Molecular Weight 55724
Enzyme 10 Theoretical pI 6.18
Enzyme 10 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 10 General Function Energy production and conversion
Enzyme 10 Specific Function Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-104
Enzyme 10 Transmembrane Regions
  • 42-62 88-108 119-139 217-237 257-277 298-318 328-348 373-393 418-438
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 348012 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P43007 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name SATT_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1599 bp
ATGGAGAAGAGCAACGAGACCAACGGCTACCTTGACAGCGCTCAGGCGGGGCCTGCGGCC
GGGCCCGGAGCTCCGGGGACCGCGGCGGGACGCGCACGGCGTTGCGCGCGCTTCCTGCGG
CGCCAAGCGCTGGTGCTGCTCACCGTGTCCGGGGTGCTGGCGGGCGCGGGCCTGGGCGCG
GCGTTGCGCGGGCTCAGCCTGAGCCGCACGCAGGTCACCTACCTGGCCTTCCCCGGCGAG
ATGCTGCTCCGCATGCTGCGCATGATCATCCTGCCGCTGGTGGTCTGCAGCCTGGTGTCG
GGCGCCGCCTCGCTCGATGCCAGCTGCCTCGGGCGTCTGGGCGGCATCCGTGTCGCCTAC
TTTGGCCTCACCACACTGAGTGCCTCGGCGCTCGCCGTGGCCTTGGCGTTCATCATCAAG
CCAGGATCCGGTGCGCAGACCCTTCAGTCCAGCGACCTGGGGCTGGAGGACTCGGGGCCT
CCTCCTGTCCCCAAAGAGACGGTGGACTCTTTCCTCGACCTGGCCAGAAACCTGTTTCCC
TCCAATCTTGTGGTTGCAGCTTTCCGTACGTATGCAACCGATTATAAAGTCGTGACCCAG
AACAGCAGCTCTGGAAATGTAACCCATGAAAAGATCCCCATAGGCACTGAGATAGAAGGG
ATGAACATTTTAGGATTGGTCCTGTTTGCTCTGGTGTTAGGAGTGGCCTTAAAGAAACTA
GGCTCCGAAGGAGAAGACCTCATCCGTTTCTTCAATTCCCTCAACGAGGCGACGATGGTG
CTGGTGTCCTGGATTATGTGGTACGTACCTGTGGGCATCATGTTCCTTGTTGGAAGCAAG
ATCGTGGAAATGAAAGACATCATCGTGCTGGTGACCAGCCTGGGGAAATACATCTTCGCA
TCTATATTGGGCCATGTTATTCATGGAGGAATTGTTCTGCCACTTATTTATTTTGTTTTC
ACACGAAAAAACCCATTCAGATTCCTCCTGGGCCTCCTCGCCCCATTTGCGACAGCATTT
GCTACCTGCTCCAGCTCAGCGACCCTTCCCTCTATGATGAAGTGCATTGAAGAGAACAAT
GGTGTGGACAAGAGGATCAGCAGGTTTATTCTCCCCATCGGGGCCACCGTGAACATGGAC
GGAGCAGCCATCTTCCAGTGTGTGGCCGCGGTGTTCATTGCGCAACTCAACAACATAGAG
CTCAACGCAGGACAGATTTTCACCATTCTAGTGACTGCCACAGCGTCCAGTGTTGGAGCA
GCAGGCGTGCCAGCTGGAGGGGTCCTCACCATTGCCATTATCCTGGAGGCCATTGGGCTG
CCTACTCATGACCTGCCTCTGATCCTGGCTGTGGACTGGATTGTGGACCGGACCACCACG
GTGGTGAATGTGGAAGGGGATGCCCTGGGTGCAGGCATTCTCCACCACCTGAATCAGAAG
GCAACAAAGAAAGGCGAGCAGGAACTTGCTGAGGTGAAAGTGGAAGCCATCCCCAACTGC
AAGTCTGAGGAGGAGACATCGCCCCTGGTGACACACCAGAACCCCGCTGGCCCCGTGGCC
AGTGCCCCAGAACTGGAATCCAAGGAGTCGGTTCTGTGA
Enzyme 10 GenBank Gene ID L14595 Link Image
Enzyme 10 GeneCard ID SLC1A4 Link Image
Enzyme 10 GenAtlas ID SLC1A4 Link Image
Enzyme 10 HGNC ID HGNC:10942 Link Image
Enzyme 10 Chromosome Location 2
Enzyme 10 Locus 2p15-p13
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Arriza JL, Kavanaugh MP, Fairman WA, Wu YN, Murdoch GH, North RA, Amara SG: Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J Biol Chem. 1993 Jul 25;268(21):15329-32. [PubMed Link Image]
  2. Shafqat S, Tamarappoo BK, Kilberg MS, Puranam RS, McNamara JO, Guadano-Ferraz A, Fremeau RT Jr: Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters. J Biol Chem. 1993 Jul 25;268(21):15351-5. [PubMed Link Image]
  3. Hofmann K, Duker M, Fink T, Lichter P, Stoffel W: Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) and localization to chromosome 2p13-p15. Genomics. 1994 Nov 1;24(1):20-6. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 9258
Enzyme 11 Name Alanine aminotransferase 2
Enzyme 11 Synonyms
  1. ALT2
  2. Glutamic--pyruvic transaminase 2
  3. Glutamate pyruvate transaminase 2
  4. GPT 2
  5. Glutamic--alanine transaminase 2
Enzyme 11 Gene Name GPT2
Enzyme 11 Protein Sequence >Alanine aminotransferase 2
MQRAAALVRRGCGPRTPSSWGRSQSSAAAEASAVLKVRPERSRRERILTLESMNPQVKAV
EYAVRGPIVLKAGEIELELQRGIKKPFTEVIRANIGDAQAMGQQPITFLRQVMALCTYPN
LLDSPSFPEDAKKRARRILQACGGNSLGSYSASQGVNCIREDVAAYITRRDGGVPADPDN
IYLTTGASDGISTILKILVSGGGKSRTGVMIPIPQYPLYSAVISELDAIQVNYYLDEENC
WALNVNELRRAVQEAKDHCDPKVLCIINPGNPTGQVQSRKCIEDVIHFAWEEKLFLLADE
VYQDNVYSPDCRFHSFKKVLYEMGPEYSSNVELASFHSTSKGYMGECGYRGGYMEVINLH
PEIKGQLVKLLSVRLCPPVSGQAAMDIVVNPPVAGEESFEQFSREKESVLGNLAKKAKLT
EDLFNQVPGIHCNPLQGAMYAFPRIFIPAKAVEAAQAHQMAPDMFYCMKLLEETGICVVP
GSGFGQREGTYHFRMTILPPVEKLKTVLQKVKDFHINFLEKYA
Enzyme 11 Number of Residues 523
Enzyme 11 Molecular Weight 57904
Enzyme 11 Theoretical pI Not Available
Enzyme 11 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 11 General Function Amino acid transport and metabolism
Enzyme 11 Specific Function L-alanine + 2-oxoglutarate = pyruvate + L- glutamate
Enzyme 11 Pathways
Enzyme 11 Reactions
  • 2-Oxoglutarate + L-Alanine <==> L-Glutamate + Pyruvate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 19046894 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q8TD30 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ALAT2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AY029173 Link Image
Enzyme 11 GeneCard ID Not Available
Enzyme 11 GenAtlas ID GPT2 Link Image
Enzyme 11 HGNC ID HGNC:18062 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 10418
Enzyme 12 Name Selenocysteine lyase
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name SCLY
Enzyme 12 Protein Sequence >Selenocysteine lyase
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGN
PSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTS
KGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQTEVDDI
LAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGK
QRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTP
MIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCN
FSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGR
STTRAEVDLVVQDLKQAVAQLEDQA
Enzyme 12 Number of Residues 445
Enzyme 12 Molecular Weight 48179
Enzyme 12 Theoretical pI Not Available
Enzyme 12 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • metabolism
  • physiological process
Component
Enzyme 12 General Function Amino acid transport and metabolism
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • Pyridoxine 5'-phosphate + Selenocysteine --> L-Alanine + H+ + Pyridoxal 5'-phosphate + Selenide
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 14043901 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q96I15 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q96I15_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID BC007891 Link Image
Enzyme 12 GeneCard ID Not Available
Enzyme 12 GenAtlas ID SCLY Link Image
Enzyme 12 HGNC ID HGNC:18161 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 12977
Enzyme 13 Name Alanine aminotransferase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name GPT
Enzyme 13 Protein Sequence >Alanine aminotransferase
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
Enzyme 13 Number of Residues 496
Enzyme 13 Molecular Weight 54637
Enzyme 13 Theoretical pI Not Available
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function Not Available
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B0YJ18 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B0YJ18_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID Not Available
Enzyme 13 GeneCard ID B0YJ18 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 13118
Enzyme 14 Name Kynureninase
Enzyme 14 Synonyms
  1. L-kynurenine hydrolase
  2. Kynureninase
  3. L-kynurenine hydrolase, isoform CRA_a
Enzyme 14 Gene Name KYNU
Enzyme 14 Protein Sequence >Kynureninase
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
Enzyme 14 Number of Residues 307
Enzyme 14 Molecular Weight 34635
Enzyme 14 Theoretical pI 5.71
Enzyme 14 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
  • kynureninase activity
  • pyridoxal phosphate binding
  • vitamin binding
Process
  • NAD biosynthesis
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • indolalkylamine metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
  • tryptophan catabolism
  • tryptophan metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 14 General Function Amino acid transport and metabolism
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function Not Available
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 12654129 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9BVW3 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q9BVW3_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID BC000879 Link Image
Enzyme 14 GeneCard ID Q9BVW3 Link Image
Enzyme 14 GenAtlas ID KYNU Link Image
Enzyme 14 HGNC ID HGNC:6469 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 14700
Enzyme 15 Name Alanine--glyoxylate aminotransferase 2-like 2
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name AGXT2L2
Enzyme 15 Protein Sequence >Alanine--glyoxylate aminotransferase 2-like 2
MAADQRPKADTLALRQRLISSSCRLFFPEDPVKIVRAQGQYMYDEQGAEYIDCISNVAHV
GHCHPLVVQAAHEQNQVLNTNSRYLHDNIVDYAQRLSETLPEQLCVFYFLNSGSEANDLA
LRLARHYTGHQDVVVLDHAYHGHLSSLIDISPYKFRNLDGQKEWVHVAPLPDTYRGPYRE
DHPNPAMAYANEVKRVVSSAQEKGRKIAAFFAESLPSVGGQIIPPAGYFSQVAEHIRKAG
GVFVADEIQVGFGRVGKHFWAFQLQGKDFVPDIVTMGKSIGNGHPVACVAATQPVARAFE
ATGVEYFNTFGGSPVSCAVGLAVLNVLEKEQLQDHATSVGSFLMQLLGQQKIKHPIVGDV
RGVGLFIGVDLIKDEATRTPATEEAAYLVSRLKENYVLLSTDGPGRNILKFKPPMCFSLD
NARQVVAKLDAILTDMEEKVRSCETLRLQP
Enzyme 15 Number of Residues 450
Enzyme 15 Molecular Weight 49711
Enzyme 15 Theoretical pI 6.76
Enzyme 15 GO Classification
Function
  • binding
  • catalytic activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
Component
Enzyme 15 General Function Amino acid transport and metabolism
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 18027842 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q8IUZ5 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name AT2L2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >324 bp
ATGCAGCTCCTCGGGCAGCAAAAAATCAAACATCCCATCGTCGGGGATGTCAGGGGTGTT
GGGCTCTTCATTGGTGTGGATCTGATCAAAGATGAGGCCACAAGGACACCAGCAACTGAA
GAGGCTGCCTACTTGGTATCAAGGCTGAAGGAGAACTACGTTTTGCTGAGCACTGATGGC
CCTGGGAGGAACATCCTGAAGTTTAAGCCCCCAATGTGCTTCAGCCTGGACAATGCACGG
CAGGTGGTGGCAAAGCTGGATGCCATTCTGACTGACATGGAAGAGAAGGTGAGAAGTTGT
GAAACGCTGAGGCTCCAGCCCTAA
Enzyme 15 GenBank Gene ID AF318375 Link Image
Enzyme 15 GeneCard ID Q8IUZ5 Link Image
Enzyme 15 GenAtlas ID AGXT2L2 Link Image
Enzyme 15 HGNC ID HGNC:28249 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 15229
Enzyme 16 Name cDNA FLJ77866, highly similar to Homo sapiens peptidoglycan recognition protein L (PGLYRP) mRNA (Peptidoglycan recognition protein 2, isoform CRA_a)
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name PGLYRP2
Enzyme 16 Protein Sequence >cDNA FLJ77866, highly similar to Homo sapiens peptidoglycan recognition protein L (PGLYRP) mRNA (Peptidoglycan recognition protein 2, isoform CRA_a)
MAQGVLWILLGLLLWSDPGTASLPLLMDSVIQALAELEQKVPAAKTRHTASAWLMSAPNS
GPHNRLYHFLLGAWSLNATELDPCPLSPELLGLTKEVARHDVREGKEYGVVLAPDGSTVA
VEPLLAGLEAGLQGRRVINLPLDSMAAPWETGDTFPDVVAIAPDVRATSSPGLRDGSPDV
TTADIGANTPDATKGCPDVQASLPDAKAKSPPTMVDSLLAVTLAGNLGLTFLRGSQTQSH
PDLGTEGCWDQLSAPRTFTLLDPKASLLTMAFLNGALDGVILGDYLSRTPEPRPSLSHLL
SQYYGAGVARDPGFRSNFRRQNGAALTSASILAQQVWGTLVLLQRLEPVHLQLQCMSQEQ
LAQVAANATKEFTEAFLGCPAIHPRCRWGAAPYRGRPKLLQLPLGFLYVHHTYVPAPPCT
DFTRCAANMRSMQRYHQDTQGWGDIGYSFVVGSDGYVYEGRGWHWVGAHTLGHNSRGFGV
AIVGNYTAALPTEAALRTVRDTLPSCAVRAGLLRPDYALLGHRQLVRTDCPGDALFDLLR
TWPHFTATVKPRPARSVSKRSRREPPPRTLPATDLQ
Enzyme 16 Number of Residues 576
Enzyme 16 Molecular Weight 62218
Enzyme 16 Theoretical pI 7.59
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function Not Available
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 158258016 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID A8K8C7 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name A8K8C7_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1731 bp
ATGGCCCAGGGTGTCCTCTGGATCCTACTCGGATTGCTACTGTGGTCAGACCCAGGGACA
GCCTCCCTGCCCCTGCTCATGGACTCTGTCATCCAGGCCCTGGCTGAGCTGGAGCAGAAA
GTGCCAGCTGCCAAGACCAGACACACAGCTTCTGCGTGGCTGATGTCAGCTCCAAACTCT
GGCCCCCACAATCGCCTCTACCACTTCCTGCTGGGGGCATGGAGCCTCAATGCTACAGAG
TTGGATCCCTGCCCACTAAGCCCAGAGCTGTTAGGCCTGACCAAGGAGGTGGCCCGACAT
GACGTACGAGAAGGGAAGGAATATGGGGTGGTGCTGGCACCTGATGGCTCGACCGTGGCT
GTGGAGCCTCTGCTGGCGGGGCTGGAGGCAGGGCTGCAAGGGCGCAGGGTCATAAATTTG
CCCTTGGACAGCATGGCTGCCCCTTGGGAGACTGGAGATACCTTTCCAGATGTTGTGGCC
ATTGCTCCAGATGTAAGAGCCACCTCCTCCCCAGGACTCAGGGATGGCTCTCCAGATGTC
ACCACTGCAGATATTGGAGCCAACACTCCAGATGCTACAAAAGGCTGTCCAGATGTCCAA
GCTTCCTTGCCAGATGCCAAAGCCAAGTCCCCACCGACCATGGTGGACAGCCTCCTGGCA
GTCACCCTGGCTGGAAACCTGGGCCTGACCTTCCTCCGAGGTTCCCAGACCCAGAGCCAT
CCAGACCTGGGAACTGAGGGCTGCTGGGACCAGCTCTCTGCCCCTCGGACCTTTACGCTT
TTGGACCCCAAGGCATCTCTGTTAACCATGGCCTTCCTCAATGGCGCCCTGGATGGGGTC
ATCCTTGGAGACTACCTGAGCCGGACTCCTGAGCCCCGGCCATCCCTCAGCCACTTGCTG
AGCCAGTACTATGGGGCTGGGGTGGCCAGAGACCCAGGGTTCCGCAGCAACTTCCGACGG
CAGAACGGTGCTGCTCTGACTTCAGCCTCCATCCTGGCCCAGCAGGTGTGGGGAACCCTT
GTCCTTCTACAGAGGCTGGAGCCAGTACACCTCCAGCTTCAGTGCATGAGCCAAGAACAG
CTGGCCCAGGTGGCTGCCAATGCTACCAAGGAATTCACTGAGGCCTTCCTGGGATGCCCG
GCCATCCACCCCCGCTGCCGCTGGGGAGCGGCGCCTTATCGGGGCCGCCCGAAGCTGCTG
CAGCTGCCGCTGGGATTCTTGTACGTGCATCACACCTACGTGCCTGCACCACCCTGCACG
GACTTCACGCGCTGCGCAGCCAACATGCGCTCCATGCAGCGCTACCACCAGGACACGCAA
GGCTGGGGAGACATCGGCTACAGTTTCGTGGTGGGCTCGGACGGCTACGTGTACGAGGGA
CGCGGCTGGCACTGGGTGGGCGCCCACACGCTCGGCCACAACTCCCGGGGCTTCGGCGTG
GCCATAGTGGGCAACTACACCGCGGCGCTGCCCACCGAGGCCGCTCTGCGCACGGTGCGC
GACACGCTCCCGAGTTGTGCGGTGCGCGCCGGCCTCCTGCGGCCAGACTACGCGCTGCTG
GGCCACCGCCAGCTGGTGCGCACCGACTGCCCCGGCGACGCGCTCTTCGACCTGCTGCGC
ACCTGGCCGCACTTCACCGCGACTGTTAAGCCAAGACCTGCCAGGAGTGTCTCTAAGAGA
TCCAGGAGGGAGCCACCCCCAAGGACCCTGCCAGCCACAGACCTCCAATAA
Enzyme 16 GenBank Gene ID AK292292 Link Image
Enzyme 16 GeneCard ID A8K8C7 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location 19
Enzyme 16 Locus 19p13.12
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15230
Enzyme 17 Name Peptidoglycan recognition protein I-alpha
Enzyme 17 Synonyms
  1. PGRP-I-alpha
  2. Peptidoglycan recognition protein intermediate alpha
  3. PGLYRPIalpha
  4. Peptidoglycan recognition protein 3
Enzyme 17 Gene Name PGLYRP3
Enzyme 17 Protein Sequence >Peptidoglycan recognition protein I-alpha
MGTLPWLLAFFILGLQAWDTPTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQ
SVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISLGIAF
FGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLLLKEETCLDPQHPVMPRKVCPN
IIKRSAWEARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDI
GYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQC
AVVEGYLTPNYLLMGHSDVVNILSPGQALYNIISTWPHFKH
Enzyme 17 Number of Residues 341
Enzyme 17 Molecular Weight 37612
Enzyme 17 Theoretical pI 6.96
Enzyme 17 GO Classification
Function
  • N-acetylmuramoyl-L-alanine amidase activity
  • binding
  • 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 linear amides
  • protein binding
Process
  • carbohydrate metabolism
  • cellular carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • peptidoglycan catabolism
  • peptidoglycan metabolism
  • physiological process
Component
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Binds to murein peptidoglycans (PGN) of Gram-positive bacteria. May play a role in innate immunity
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-17
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 15590684 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q96LB9 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PGRP3_HUMAN Link Image
Enzyme 17 PDB ID 1SK3 Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1026 bp
ATGGGGACGCTGCCATGGCTTCTTGCCTTCTTCATTCTGGGTCTCCAGGCTTGGGATACT
CCCACCATCGTCTCCCGCAAGGAGTGGGGGGCAAGACCGCTCGCCTGCAGGGCCCTGCTG
ACCCTGCCTGTGGCCTACATCATCACAGACCAGCTCCCAGGGATGCAGTGCCAGCAGCAG
AGCGTTTGCAGCCAGATGCTGCGGGGGTTGCAGTCCCATTCCGTCTACACCATAGGCTGG
TGCGACGTGGCGTACAACTTCCTGGTTGGGGATGATGGCAGGGTGTATGAAGGTGTTGGC
TGGAACATCCAAGGCTTGCACACCCAGGGCTACAACAACATTTCCCTGGGCATCGCCTTC
TTTGGCAATAAGATAGGCAGCAGTCCCAGCCCTGCTGCCTTATCAGCTGCAGAGGGTCTG
ATCTCCTATGCCATCCAGAAGGGTCACCTGTCGCCCAGGTATATTCAGCCACTTCTTCTG
AAAGAAGAGACCTGCCTGGACCCTCAACATCCAGTGATGCCCAGGAAGGTTTGCCCCAAC
ATCATCAAACGATCTGCTTGGGAAGCCAGAGAGACACACTGCCCTAAAATGAACCTCCCA
GCCAAATATGTCATCATCATCCACACCGCTGGCACAAGCTGCACTGTATCCACAGACTGC
CAGACTGTCGTCCGAAACATACAGTCCTTTCACATGGACACACGGAACTTTTGTGACATT
GGATATCACTTCCTGGTGGGCCAGGATGGTGGCGTGTATGAAGGGGTTGGATGGCACATC
CAAGGCTCTCACACTTATGGATTCAACGATATTGCCCTAGGAATTGCCTTCATCGGCTAC
TTTGTAGAAAAGCCTCCAAATGCTGCAGCGCTGGAGGCGGCCCAGGACCTGATCCAGTGT
GCCGTGGTTGAGGGGTACCTGACTCCAAACTACCTGCTGATGGGCCACAGTGACGTGGTC
AACATCCTGTCCCCTGGGCAGGCTTTGTATAACATCATCAGCACCTGGCCTCATTTCAAG
CACTGA
Enzyme 17 GenBank Gene ID AY035376 Link Image
Enzyme 17 GeneCard ID Q96LB9 Link Image
Enzyme 17 GenAtlas ID PGLYRP3 Link Image
Enzyme 17 HGNC ID HGNC:30014 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Liu C, Xu Z, Gupta D, Dziarski R: Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. J Biol Chem. 2001 Sep 14;276(37):34686-94. Epub 2001 Jul 18. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 15231
Enzyme 18 Name Peptidoglycan recognition protein 4 (PGLYRP4 protein)
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name PGLYRP4
Enzyme 18 Protein Sequence >Peptidoglycan recognition protein 4 (PGLYRP4 protein)
MLPWLLVFSALGIQAWGDSSWNKTQAKQVSEGLQYLFENISQLTEKGLPTDVSTTVSRKA
WGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFL
VGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKG
HLSSSYVQPLLGKGENCLAPRQKTSLKKACPGVVPRSVWGARETHCPRMTLPAKYGIIIH
TAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVGWNVQGSSTPGY
DDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVARTLSPGQA
LYNIISTWPHFKH
Enzyme 18 Number of Residues 373
Enzyme 18 Molecular Weight 40621
Enzyme 18 Theoretical pI 7.53
Enzyme 18 GO Classification
Function
  • N-acetylmuramoyl-L-alanine amidase activity
  • binding
  • 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 linear amides
  • protein binding
Process
  • carbohydrate metabolism
  • cellular carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • peptidoglycan catabolism
  • peptidoglycan metabolism
  • physiological process
Component
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 148744335 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q5SY64 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q5SY64_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1122 bp
ATGCTGCCGTGGCTTCTTGTCTTCTCTGCTCTGGGTATCCAGGCCTGGGGTGATTCCTCC
TGGAACAAAACACAAGCTAAACAGGTATCAGAGGGGCTCCAGTACCTATTTGAGAACATC
TCCCAGCTCACTGAAAAAGGCCTTCCCACAGATGTCTCCACCACGGTCTCTCGCAAGGCA
TGGGGGGCAGAAGCTGTTGGCTGCAGTATTCAGCTGACCACGCCAGTGAATGTCCTTGTT
ATACACCATGTCCCTGGACTGGAGTGTCACGACCAGACAGTCTGCAGCCAGAGACTGCGG
GAACTGCAGGCCCATCATGTCCACAACAACAGTGGGTGTGATGTGGCCTACAACTTCCTG
GTTGGGGATGATGGCAGGGTGTATGAAGGTGTTGGCTGGAATATCCAAGGAGTGCACACC
CAAGGCTACAACAACATCTCCCTGGGCTTTGCCTTCTTTGGCACTAAGAAAGGCCACAGT
CCCAGCCCTGCTGCCCTGTCGGCCATGGAAAACCTAATCACCTATGCTGTCCAGAAGGGC
CACCTGTCATCCAGTTATGTTCAGCCACTTCTTGGGAAAGGCGAGAACTGCCTGGCCCCT
CGGCAGAAGACAAGCCTGAAGAAGGCTTGCCCCGGCGTTGTCCCACGGTCTGTGTGGGGA
GCCAGGGAGACCCACTGTCCCAGGATGACTCTCCCAGCGAAGTATGGCATCATTATCCAC
ACTGCCGGGAGGACCTGCAACATTTCTGATGAGTGCCGCCTGCTGGTCCGGGACATCCAG
TCTTTCTACATAGACAGGCTCAAGTCATGCGACATTGGTTATAACTTCCTGGTGGGCCAG
GATGGCGCCATTTATGAAGGGGTGGGCTGGAATGTCCAAGGCTCCTCCACCCCTGGCTAC
GATGACATTGCCCTGGGCATTACCTTCATGGGCACCTTCACAGGTATACCACCCAATGCT
GCAGCACTAGAGGCAGCCCAAGACCTGATCCAGTGTGCCATGGTCAAAGGGTACCTGACT
CCCAACTACCTGCTGGTGGGCCACAGTGATGTGGCCCGAACCTTGTCTCCTGGGCAGGCT
TTGTACAACATCATCAGCACCTGGCCTCATTTCAAACACTGA
Enzyme 18 GenBank Gene ID BC142636 Link Image
Enzyme 18 GeneCard ID Q5SY64 Link Image
Enzyme 18 GenAtlas ID PGLYRP4 Link Image
Enzyme 18 HGNC ID HGNC:30015 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16505
Enzyme 19 Name cDNA FLJ10608 fis, clone NT2RP2005239, highly similar to Cysteine desulfurase, mitochondrial (EC 2.8.1.7)
Enzyme 19 Synonyms
  1. SubName: NFS1 nitrogen fixation 1 (S. cerevisiae), isoform CRA_a
Enzyme 19 Gene Name NFS1
Enzyme 19 Protein Sequence >cDNA FLJ10608 fis, clone NT2RP2005239, highly similar to Cysteine desulfurase, mitochondrial (EC 2.8.1.7)
MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
Enzyme 19 Number of Residues 457
Enzyme 19 Molecular Weight 50196
Enzyme 19 Theoretical pI 8.45
Enzyme 19 GO Classification
Function
  • binding
  • catalytic activity
  • cysteine desulfurase activity
  • pyridoxal phosphate binding
  • sulfurtransferase activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • transferase activity, transferring sulfur-containing groups
  • vitamin binding
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • cysteine metabolism
  • metabolism
  • physiological process
  • sulfur amino acid metabolism
Component
Enzyme 19 General Function Amino acid transport and metabolism
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine ALL_REAC (other) R07460
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID B3KMA5 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name B3KMA5_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AK001470 Link Image
Enzyme 19 GeneCard ID B3KMA5 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location 20
Enzyme 19 Locus 20q11.22
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16929
Enzyme 20 Name Probable alanyl-tRNA synthetase, mitochondrial
Enzyme 20 Synonyms
  1. Alanine--tRNA ligase
  2. AlaRS
  3. Alanyl-tRNA synthetase-like
Enzyme 20 Gene Name AARS2
Enzyme 20 Protein Sequence >Probable alanyl-tRNA synthetase, mitochondrial
MAASVAAAARRLRRAIRRSPAWRGLSHRPLSSEPPAAKASAVRAAFLNFFRDRHGHRLVP
SASVRPRGDPSLLFVNAGMNQFKPIFLGTVDPRSEMAGFRRVANSQKCVRAGGHHNDLED
VGRDLSHHTFFEMLGNWAFGGEYFKEEACNMAWELLTQVYGIPEERLWISYFDGDPKAGL
DPDLETRDIWLSLGVPASRVLSFGPQENFWEMGDTGPCGPCTEIHYDLAGGVGAPQLVEL
WNLVFMQHNREADGSLQPLPQRHVDTGMGLERLVAVLQGKHSTYDTDLFSPLLNAIQQGC
RAPPYLGRVGVADEGRTDTAYRVVADHIRTLSVCISDGIFPGMSGPPLVLRRILRRAVRF
SMEILKAPPGFLGSLVPVVVETLGDAYPELQRNSAQIANLVSEDEAAFLASLERGRRIID
RTLRTLGPSDMFPAEVAWSLSLCGDLGLPLDMVELMLEEKGVQLDSAGLERLAQEEAQHR
ARQAEPVQKQGLWLDVHALGELQRQGVPPTDDSPKYNYSLRPSGSYEFGTCEAQVLQLYT
EDGTAVASVGKGQRCGLLLDRTNFYAEQGGQASDRGYLVRAGQEDVLFPVARAQVCGGFI
LHEAVAPECLRLGDQVQLHVDEAWRLGCMAKHTATHLLNWALRQTLGPGTEQQGSHLNPE
QLRLDVTTQTPLTPEQLRAVENTVQEAVGQDEAVYMEEVPLALTAQVPGLRSLDEVYPDP
VRVVSVGVPVAHALDPASQAALQTSVELCCGTHLLRTGAVGDLVIIGDRQLSKGTTRLLA
VTGEQAQQARELGQSLAQEVKAATERLSLGSRDVAEALRLSKDIGRLIEAVETAVMPQWQ
RRELLATVKMLQRRANTAIRKLQMGQAAKKTQELLERHSKGPLIVDTVSAESLSVLVKVV
RQLCEQAPSTSVLLLSPQPMGKVLCACQVAQGAMPTFTAEAWALAVCSHMGGKAWGSRVV
AQGTGSTTDLEAALSIAQTYALSQL
Enzyme 20 Number of Residues 985
Enzyme 20 Molecular Weight 107342
Enzyme 20 Theoretical pI 6.20
Enzyme 20 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • alanine-tRNA ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • alanyl-tRNA aminoacylation
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
Enzyme 20 General Function Translation, ribosomal structure and biogenesis
Enzyme 20 Specific Function ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID Q5JTZ9 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name SYAM_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AB033096 Link Image
Enzyme 20 GeneCard ID Q5JTZ9 Link Image
Enzyme 20 GenAtlas ID AARS2 Link Image
Enzyme 20 HGNC ID HGNC:21022 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [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 20 Metabolite References Not Available