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Human Metabolome Database Version 2.5

 

Showing metabocard for Flavin Mononucleotide (HMDB01520)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-07 14:40:29
Accession Number HMDB01520
Secondary Accession Numbers Not Available
Common Name Flavin Mononucleotide
Description A coenzyme for a number of oxidative enzymes including NADH dehydrogenase. It is the principal form in which riboflavin is found in cells and tissues.
Synonyms
  1. FMN
  2. Flanin
  3. Flavine mononucleotide
  4. Flavol
  5. Riboflavin
  6. Riboflavin 5'-monophosphate
  7. Riboflavin 5'-phosphate
  8. Riboflavin Mononucleotide
  9. Riboflavin monophosphate
  10. Riboflavin phosphate
  11. Riboflavin-5'-phosphate na
  12. Riboflavin-5-phosphate
  13. Riboflavine 5'-monophosphate
  14. Riboflavine 5'-phosphate
  15. Riboflavine dihydrogen phosphate
  16. Riboflavine monophosphate
  17. Riboflavine phosphate
  18. Riboflavine-5'-phosphate
  19. Vitamin B2 phosphate
Chemical IUPAC Name Riboflavin 5'-(dihydrogen phosphate)
Chemical Formula C17H21N4O9P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellanous
Class
  • Pterins
Sub Class
  • Miscellaneous heterocyclic compounds
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Riboflavin metabolism
Application
Source
  • Endogenous
Average Molecular Weight 456.344
Monoisotopic Molecular Weight 456.104614
Isomeric SMILES CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)COP(O)(O)=O)C1=NC(=O)NC(=O)C1=N2
Canonical SMILES CC1=CC2=C(C=C1C)N(CC(O)C(O)C(O)COP(O)(O)=O)C1=NC(=O)NC(=O)C1=N2
KEGG Compound ID C00061 Link Image
BioCyc ID FMN Link Image
BiGG ID 33703 Link Image
Wikipedia Link FMN Link Image
NuGOwiki Link HMDB01520 Link Image
Metagene Link HMDB01520 Link Image
METLIN ID 6295 Link Image
PubChem Compound 710 Link Image
PubChem Substance 7988671 Link Image
ChEBI ID 17621 Link Image
CAS Registry Number 146-17-8
InChI Identifier InChI=1/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
Synthesis Reference Ono, Shigeru; Hirano, Hiroko; Sato, Yoshiyuki. Formation of flavin adenine dinucleotide and flavin mononucleotide by lens homogenate. Experimental Eye Research (1982), 34(2), 297-301.
Melting Point (Experimental) 290 oC
Experimental Water Solubility 92 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 2.0 mg/mL [MEYLAN,WM et al. (1996)]; 0.668 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.78 [Predicted by ALOGPS]; -3.1 [Predicted by PubChem via XLOGP]; -1.73 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1AG9 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 Not Available
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 Not Available
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
Tissue Location
Tissue References
Erythrocyte
Eye Lens
Muscle
Platelet
Concentrations (Normal)
Biofluid Blood
Value 0.016 +/- 0.009 uM
Age Adolescent:13-18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Capo-chichi CD, Gueant JL, Lefebvre E, Bennani N, Lorentz E, Vidailhet C, Vidailhet M: Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-8. [PubMed Link Image]
Biofluid Blood
Value 0.0075 (0.004-0.011) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hustad S, McKinley MC, McNulty H, Schneede J, Strain JJ, Scott JM, Ueland PM: Riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in human plasma and erythrocytes at baseline and after low-dose riboflavin supplementation. Clin Chem. 2002 Sep;48(9):1571-7. [PubMed Link Image]
Biofluid Blood
Value 0.0084 (0.0035-0.013) uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Fabian E, Majchrzak D, Dieminger B, Meyer E, Elmadfa I: Influence of probiotic and conventional yoghurt on the status of vitamins B1, B2 and B6 in young healthy women. Ann Nutr Metab. 2008;52(1):29-36. Epub 2008 Jan 30. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.012 +/- 0.006 uM
Age Adolescent:13-18 yrs old
Sex Female
Condition Anorexia nervosa
Comments Not Available
References
  • Capo-chichi CD, Gueant JL, Lefebvre E, Bennani N, Lorentz E, Vidailhet C, Vidailhet M: Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-8. [PubMed Link Image]
Biofluid Blood
Value 0.013 +/- 0.006 uM
Age Children:1-13 yrs old
Sex Both
Comments Not Available
References
  • Capo-Chichi CD, Feillet F, Gueant JL, Amouzou K, Zonon N, Sanni A, Lefebvre E, Assimadi K, Vidailhet M: Concentrations of riboflavin and related organic acids in children with protein-energy malnutrition. Am J Clin Nutr. 2000 Apr;71(4):978-86. [PubMed Link Image]
Associated Disorders
Condition References
Anorexia nervosa
  • Capo-chichi CD, Gueant JL, Lefebvre E, Bennani N, Lorentz E, Vidailhet C, Vidailhet M: Riboflavin and riboflavin-derived cofactors in adolescent girls with anorexia nervosa. Am J Clin Nutr. 1999 Apr;69(4):672-8. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Riboflavin Metabolism SMP00070 Link Image map00740 Link Image
General References
  1. Mathew JL, Kabi BC, Rath B: Anti-oxidant vitamins and steroid responsive nephrotic syndrome in Indian children. J Paediatr Child Health. 2002 Oct;38(5):450-37. [PubMed Link Image]
  2. Edelbroek PM, Linssen AC, Zitman FG, Rooymans HG, de Wolff FA: Analgesic and antidepressive effects of low-dose amitriptyline in relation to its metabolism in patients with chronic pain. Clin Pharmacol Ther. 1986 Feb;39(2):156-62. [PubMed Link Image]
  3. Booth CK, Clark T, Fenn A: Folic acid, riboflavin, thiamine, and vitamin B-6 status of a group of first-time blood donors. Am J Clin Nutr. 1998 Nov;68(5):1075-80. [PubMed Link Image]
  4. Ahmed F, Khan MR, Akhtaruzzaman M, Karim R, Marks GC, Banu CP, Nahar B, Williams G: Efficacy of twice-weekly multiple micronutrient supplementation for improving the hemoglobin and micronutrient status of anemic adolescent schoolgirls in Bangladesh. Am J Clin Nutr. 2005 Oct;82(4):829-35. [PubMed Link Image]
  5. Mikalunas V, Fitzgerald K, Rubin H, McCarthy R, Craig RM: Abnormal vitamin levels in patients receiving home total parenteral nutrition. J Clin Gastroenterol. 2001 Nov-Dec;33(5):393-6. [PubMed Link Image]
  6. Buzina R, Grgic Z, Jusic M, Sapunar J, Milanovic N, Brubacher G: Nutritional status and physical working capacity. Hum Nutr Clin Nutr. 1982;36(6):429-38. [PubMed Link Image]
  7. Ortega RM, Quintas ME, Martinez RM, Andres P, Lopez-Sobaler AM, Requejo AM: Riboflavin levels in maternal milk: the influence of vitamin B2 status during the third trimester of pregnancy. J Am Coll Nutr. 1999 Aug;18(4):324-9. [PubMed Link Image]
  8. Baeckert PA, Greene HL, Fritz I, Oelberg DG, Adcock EW: Vitamin concentrations in very low birth weight infants given vitamins intravenously in a lipid emulsion: measurement of vitamins A, D, and E and riboflavin. J Pediatr. 1988 Dec;113(6):1057-65. [PubMed Link Image]
  9. Bamji MS, Bhaskaram P, Jacob CM: Urinary riboflavin excretion and erythrocyte glutathione reductase activity in preschool children suffering from upper respiratory infections and measles. Ann Nutr Metab. 1987;31(3):191-6. [PubMed Link Image]
  10. Lartey A, Manu A, Brown KH, Dewey KG: Predictors of micronutrient status among six- to twelve-month-old breast-fed Ghanaian infants. J Nutr. 2000 Feb;130(2):199-207. [PubMed Link Image]
  11. Ajayi OA: Bioavailability of riboflavin from fortified palm juice. Plant Foods Hum Nutr. 1989 Dec;39(4):375-80. [PubMed Link Image]
  12. Blajchman MA, Goldman M, Baeza F: Improving the bacteriological safety of platelet transfusions. Transfus Med Rev. 2004 Jan;18(1):11-24. [PubMed Link Image]
  13. Brun TA, Chen J, Campbell TC, Boreham J, Feng Z, Parpia B, Shen TF, Li M: Urinary riboflavin excretion after a load test in rural China as a measure of possible riboflavin deficiency. Eur J Clin Nutr. 1990 Mar;44(3):195-206. [PubMed Link Image]
  14. Rao PN, Levine E, Myers MO, Prakash V, Watson J, Stolier A, Kopicko JJ, Kissinger P, Raj SG, Raj MH: Elevation of serum riboflavin carrier protein in breast cancer. Cancer Epidemiol Biomarkers Prev. 1999 Nov;8(11):985-90. [PubMed Link Image]
  15. Zhou X, Huang C, Hong J, Yao S: [Nested case-control study on riboflavin levels in blood and urine and the risk of lung cancer] Wei Sheng Yan Jiu. 2003 Nov;32(6):597-8, 601. [PubMed Link Image]
  16. Thurnham DI, Zheng SF, Munoz N, Crespi M, Grassi A, Hambidge KM, Chai TF: Comparison of riboflavin, vitamin A, and zinc status of Chinese populations at high and low risk for esophageal cancer. Nutr Cancer. 1985;7(3):131-43. [PubMed Link Image]
  17. Bates CJ, Prentice AM, Paul AA, Prentice A, Sutcliffe BA, Whitehead RG: Riboflavin status in infants born in rural Gambia, and the effect of a weaning food supplement. Trans R Soc Trop Med Hyg. 1982;76(2):253-8. [PubMed Link Image]
  18. Cikot RJ, Steegers-Theunissen RP, Thomas CM, de Boo TM, Merkus HM, Steegers EA: Longitudinal vitamin and homocysteine levels in normal pregnancy. Br J Nutr. 2001 Jan;85(1):49-58. [PubMed Link Image]
  19. Hardwick CC, Herivel TR, Hernandez SC, Ruane PH, Goodrich RP: Separation, identification and quantification of riboflavin and its photoproducts in blood products using high-performance liquid chromatography with fluorescence detection: a method to support pathogen reduction technology. Photochem Photobiol. 2004 Nov-Dec;80(3):609-15. [PubMed Link Image]
  20. Schorah CJ, Wild J, Hartley R, Sheppard S, Smithells RW: The effect of periconceptional supplementation on blood vitamin concentrations in women at recurrence risk for neural tube defect. Br J Nutr. 1983 Mar;49(2):203-11. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Tartrate-resistant acid phosphatase type 5 precursor
  2. Prostatic acid phosphatase precursor
  3. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  4. Lathosterol oxidase
  5. NADPH--cytochrome P450 reductase
  6. Dihydroorotate dehydrogenase, mitochondrial precursor
  7. NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor
  8. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
  9. Methionine synthase reductase, mitochondrial precursor
  10. Pyridoxine-5'-phosphate oxidase
  11. Dihydropyrimidine dehydrogenase [NADP+] precursor
  12. Hydroxyacid oxidase 1
  13. Hydroxyacid oxidase 2
  14. Nitric oxide synthase, inducible
  15. Nitric-oxide synthase, brain
  16. Nitric-oxide synthase, endothelial
  17. Riboflavin kinase
  18. Phosphopantothenoylcysteine decarboxylase
  19. Lysophosphatidic acid phosphatase type 6 precursor
  20. Growth-inhibiting protein 16
  21. FAD synthetase
  22. NADPH-dependent FMN and FAD containing oxidoreductase
  23. Iodotyrosine dehalogenase 1 precursor
  24. tRNA wybutosine-synthesizing protein 1 homolog
  25. tRNA wybutosine-synthesizing protein 1 homolog B
  26. cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a)
  27. Testicular acid phosphatase
  28. Sarcosine dehydrogenase
  29. Putative uncharacterized protein ACP1
Enzyme 1 [top]
Enzyme 1 ID 5329
Enzyme 1 Name Tartrate-resistant acid phosphatase type 5 precursor
Enzyme 1 Synonyms
  1. TR- AP
  2. Tartrate-resistant acid ATPase
  3. TrATPase
  4. Acid phosphatase 5, tartrate resistant
Enzyme 1 Gene Name ACP5
Enzyme 1 Protein Sequence >Tartrate-resistant acid phosphatase type 5 precursor
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQI
LGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQ
IAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKL
ARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGH
DHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSK
EMTVTYIEASGKSLFKTRLPRRARP
Enzyme 1 Number of Residues 325
Enzyme 1 Molecular Weight 36599
Enzyme 1 Theoretical pI 8.95
Enzyme 1 GO Classification
Function
  • acid phosphatase activity
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • iron ion binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
  • transition metal ion binding
Process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-21
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 178006 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P13686 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PPA5_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >972 bp
ATGGACATGTGGACGGCGCTGCTCATCCTGCAAGCCTTGTTGCTACCCTCCCTGGCTGAT
GGTGCCACCCCTGCCCTGCGCTTTGTAGCCGTGGGTGACTGGGGAGGGGTCCCCAATGCC
CCATTCCACACGGGCCCGGAAATGGCCAATGCCAAGGAGATCGCTCGGACTGTGCAGATC
CTGGGTGCAGACTTCATCCTGTCTCTAGGGGACAATTTTTACTTCACTGGTGTGCAAGAC
ATCAATGACAAGAGGTTCCAGGAGACCTTTGAGGACGTATTCTCTGACCGCTCCCTTCGC
AAAGTGCCCTGGTACGTGCTAGCCGGAAACCATGACCACCTTGGCAATGTCTCTGCCCAG
ATTGCATACTCTAAGATCTCCAAGCGCTGGAACTTCCCCAGCCCTTTCTACCGCCTGCAC
TTCAAGATCCCACAGACCAATGTGTCTGTGGCCATTTTTATGCTGGACACAGTGACACTA
TGTGGCAACTCAGATGACTTCCTCAGCCAGCAGCCTGAGAGGCCCCGACTAACTGCCCGC
ACACAGCTGTCCTGGCTCAAGAAACAGCTGGCGGCGGCCAGGGAGGACTACGTGCTGGTG
GCTGGCCACTACCCCGTGTGGTCCATAGCCGAGCACGGGCCTACCCACTGCCTGGTCAAG
CAGCTACGGCCACTGCTGGCCACATACGGGGTCACTGCCTACCTGTGCGGCCACGATCAC
AATCTGCAGTACCTGCAAGATGAGAATGGCGTGGGCTACGTGCTGAGTGGGGCTGGGAAT
TTCATGGACCCCTCAAAGCGGCACCAGCGCAAGGTCCCCAACGGCTATCTGCGCTTCCAC
TATGGGACTGAAGACTCACTGGGTGGCTTTGCCTATGTGGAGATCAGCTCCAAAGAGATG
ACTGTCACTTACATCGAGGCCTCGGGCAAGTCCCTCTTTAAGACCAGGCTGCCGAGGCGA
GCCAGGCCCTGA
Enzyme 1 GenBank Gene ID J04430 Link Image
Enzyme 1 GeneCard ID ACP5 Link Image
Enzyme 1 GenAtlas ID ACP5 Link Image
Enzyme 1 HGNC ID HGNC:124 Link Image
Enzyme 1 Chromosome Location 19
Enzyme 1 Locus 19p13.3-p13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ketcham CM, Roberts RM, Simmen RC, Nick HS: Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989 Jan 5;264(1):557-63. [PubMed Link Image]
  2. Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM: Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93. [PubMed Link Image]
  3. Cassady AI, King AG, Cross NC, Hume DA: Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993 Aug 25;130(2):201-7. [PubMed Link Image]
  4. Stepan JJ, Lau KH, Mohan S, Kraenzlin M, Baylink DJ: Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1027-34. [PubMed Link Image]
  5. Stepan JJ, Lau KH, Mohan S, Singer FR, Baylink DJ: Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure. Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. [PubMed Link Image]
  6. Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ: Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989 Jul 15;261(2):601-9. [PubMed Link Image]
  7. Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. Biochem J. 1991 Aug 1;277 ( Pt 3):631-4. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5330
Enzyme 2 Name Prostatic acid phosphatase precursor
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name ACPP
Enzyme 2 Protein Sequence >Prostatic acid phosphatase precursor
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKE
SSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNL
AALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKR
LHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSE
LSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMAL
DVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELV
GPVIPQDWSTECMTTNSHQGTEDSTD
Enzyme 2 Number of Residues 386
Enzyme 2 Molecular Weight 44567
Enzyme 2 Theoretical pI 6.19
Enzyme 2 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
Component
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-32
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 189613 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P15309 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PPAP_HUMAN Link Image
Enzyme 2 PDB ID 1ND6 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1161 bp
ATGAGAGCTGCACCCCTCCTCCTGGCCAGGGCAGCAAGCCTTAGCCTTGGCTTCTTGTTT
CTGCTTTTTTTCTGGCTAGACCGAAGTGTACTAGCCAAGGAGTTGAAGTTTGTGACTTTG
GTGTTTCGGCATGGAGACCGAAGTCCCATTGACACCTTTCCCACTGACCCCATAAAGGAA
TCCTCATGGCCACAAGGATTTGGCCAACTCACCCAGCTGGGCATGGAGCAGCATTATGAA
CTTGGAGAGTATATAAGAAAGAGATATAGAAAATTCTTGAATGAGTCCTATAAACATGAA
CAGGTTTATATTCGAAGCACAGACGTTGACCGGACTTTGATGAGTGCTATGACAAACCTG
GCAGCCCTGTTTCCCCCAGAAGGTGTCAGCATCTGGAATCCTATCCTACTCTGGCAGCCC
ATCCCGGTGCACACAGTTCCTCTTTCTGAAGATCAGTTGCTATACCTGCCTTTCAGGAAC
TGCCCTCGTTTTCAAGAACTTGAGAGTGAGACTTTGAAATCAGAGGAATTCCAGAAGAGG
CTGCACCCTTATAAGGATTTTATAGCTACCTTGGGAAAACTTTCAGGATTACATGGCCAG
GACCTTTTTGGAATTTGGAGTAAAGTCTACGACCCTTTATATTGTGAGAGTGTTCACAAT
TTCACTTTACCCTCCTGGGCCACTGAGGACACCATGACTAAGTTGAGAGAATTGTCAGAA
TTGTCCCTCCTGTCCCTCTATGGAATTCACAAGCAGAAAGAGAAATCTAGGCTCCAAGGG
GGTGTCCTGGTCAATGAAATCCTCAATCACATGAAGAGAGCAACTCAGATACCAAGCTAC
AAAAAACTTATCATGTATTCTGCGCATGACACTACTGTGAGTGGCCTACAGATGGCGCTA
GATGTTTACAACGGACTCCTTCCTCCCTATGCTTCTTGCCACTTGACGGAATTGTACTTT
GAGAAGGGGGAGTACTTTGTGGAGATGTACTACCGGAATGAGACGCAGCACGAGCCGTAT
CCCCTCATGCTACCTGGCTGCAGCCCCAGCTGTCCTCTGGAGAGGTTTGCTGAGCTGGTT
GGCCCTGTGATCCCTCAAGACTGGTCCACGGAGTGTATGACCACAAACAGCCATCAAGGT
ACTGAGGACAGTACAGATTAG
Enzyme 2 GenBank Gene ID M97589 Link Image
Enzyme 2 GeneCard ID ACPP Link Image
Enzyme 2 GenAtlas ID ACPP Link Image
Enzyme 2 HGNC ID HGNC:125 Link Image
Enzyme 2 Chromosome Location 3
Enzyme 2 Locus 3q21-q23
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Sharief FS, Li SS: Structure of human prostatic acid phosphatase gene. Biochem Biophys Res Commun. 1992 May 15;184(3):1468-76. [PubMed Link Image]
  2. Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL: Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem. 1991 Feb 5;266(4):2313-9. [PubMed Link Image]
  3. Sharief FS, Lee H, Leuderman MM, Lundwall A, Deaven LL, Lee CL, Li SS: Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989 Apr 14;160(1):79-86. [PubMed Link Image]
  4. Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML: Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988 Aug 29;236(2):275-81. [PubMed Link Image]
  5. Tailor PG, Govindan MV, Patel PC: Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. Nucleic Acids Res. 1990 Aug 25;18(16):4928. [PubMed Link Image]
  6. Sharief FS, Li SS: Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. Biochem Mol Biol Int. 1994 Jun;33(3):561-5. [PubMed Link Image]
  7. LaCount MW, Handy G, Lebioda L: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. J Biol Chem. 1998 Nov 13;273(46):30406-9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5351
Enzyme 3 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 3 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. NPPase]
Enzyme 3 Gene Name ENPP1
Enzyme 3 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 3 Number of Residues 925
Enzyme 3 Molecular Weight 104925
Enzyme 3 Theoretical pI 7.14
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 77-97
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 189650 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2622 bp
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 3 GenBank Gene ID M57736 Link Image
Enzyme 3 GeneCard ID ENPP1 Link Image
Enzyme 3 GenAtlas ID ENPP1 Link Image
Enzyme 3 HGNC ID HGNC:3356 Link Image
Enzyme 3 Chromosome Location 6
Enzyme 3 Locus 6q22-q23
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. 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]
  4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5367
Enzyme 4 Name Lathosterol oxidase
Enzyme 4 Synonyms
  1. Lathosterol 5-desaturase
  2. Delta(7-sterol 5-desaturase
  3. C-5 sterol desaturase
  4. Sterol-C5- desaturase
Enzyme 4 Gene Name SC5DL
Enzyme 4 Protein Sequence >Lathosterol oxidase
MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE
Enzyme 4 Number of Residues 299
Enzyme 4 Molecular Weight 35301
Enzyme 4 Theoretical pI 8.24
Enzyme 4 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 32-52 79-99 117-137 186-206
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1906796 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O75845 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SC5D_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >711 bp
ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTAAGAATGAAAAATTAT
TCAATGGAGAGTTTACAAAGACTGAATAGATTATTGCCCAGTTATTCTTAA
Enzyme 4 GenBank Gene ID D85181 Link Image
Enzyme 4 GeneCard ID SC5DL Link Image
Enzyme 4 GenAtlas ID SC5DL Link Image
Enzyme 4 HGNC ID HGNC:10547 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11q23.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed Link Image]
  2. Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed Link Image]
  3. Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed Link Image]
  4. Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed Link Image]
  5. Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5415
Enzyme 5 Name NADPH--cytochrome P450 reductase
Enzyme 5 Synonyms
  1. CPR
  2. P450R
Enzyme 5 Gene Name POR
Enzyme 5 Protein Sequence >NADPH--cytochrome P450 reductase
MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTL
TSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLA
DLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEH
FNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEES
SIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHL
MHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHP
FPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWV
VEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYET
KAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPF
IGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQS
HKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVD
YIKKLMTKGRYSLDVWS
Enzyme 5 Number of Residues 677
Enzyme 5 Molecular Weight 76691
Enzyme 5 Theoretical pI 5.28
Enzyme 5 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 5 General Function Inorganic ion transport and metabolism
Enzyme 5 Specific Function This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-39
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 247307 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P16435 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NCPR_HUMAN Link Image
Enzyme 5 PDB ID 1AMO Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2031 bp
GGAGACTCCCACGTGGACACCAGCTCCACCGTGTCCGAGGCGGTGGCCGAAGAAGTATCT
CTTTTCAGCATGACGGACATGATTCTGTTTTCGCTCATCGTGGGTCTCCTAACCTACTGG
TTCCTCTTCAGAAAGAAAAAAGAAGAAGTCCCCGAGTTCACCAAAATTCAGACATTGACC
TCCTCTGTCAGAGAGAGCAGCTTTGTGGAAAAGATGAAGAAAACGGGGAGGAACATCATC
GTGTTCTACGGCTCCCAGACGGGGACTGCAGAGGAGTTTGCCAACCGCCTGTCCAAGGAC
GCCCACCGCTACGGGATGCGAGGCATGTCAGCGGACCCTGAGGAGTATGACCTGGCCGAC
CTGAGCAGCCTGCCAGAGATCGACAACGCCCTGGTGGTTTTCTGCATGGCCACCTACGGT
GAGGGAGACCCCACCGACAATGCCCAGGACTTCTACGACTGGCTGCAGGAGACAGACGTG
GATCTCTCTGGGGTCAAGTTCGCGGTGTTTGGTCTTGGGAACAAGACCTACGAGCACTTC
AATGCCATGGGCAAGTACGTGGACAAGCGGCTGGAGCAGCTCGGCGCCCAGCGCATCTTT
GAGCTGGGGTTGGGCGACGACGATGGGAACTTGGAGGAGGACTTCATCACCTGGCGAGAG
CAGTTCTGGCCGGCCGTGTGTGAACACTTTGGGGTGGAAGCCACTGGCGAGGAGTCCAGC
ATTCGCCAGTACGAGCTTGTGGTCCACACCGACATAGATGCGGCCAAGGTGTACATGGGG
GAGATGGGCCGGCTGAAGAGCTACGAGAACCAGAAGCCCCCCTTTGATGCCAAGAATCCG
TTCCTGGCTGCAGTCACCACCAACCGGAAGCTGAACCAGGGAACCGAGCGCCACCTCATG
CACCTGGAATTGGACATCTCGGACTCCAAAATCAGGTATGAATCTGGGGACCACGTGGCT
GTGTACCCAGCCAACGACTCTGCTCTCGTCAACCAGCTGGGCAAAATCCTGGGTGCCGAC
CTGGACGTCGTCATGTCCCTGAACAACCTGGATGAGGAGTCCAACAAGAAGCACCCATTC
CCGTGCCCTACGTCCTACCGCACGGCCCTCACCTACTACCTGGACATCACCAACCCGCCG
CGTACCAACGTGCTGTACGAGCTGGCGCAGTACGCCTCGGAGCCCTCGGAGCAGGAGCTG
CTGCGCAAGATGGCCTCCTCCTCCGGCGAGGGCAAGGAGCTGTACCTGAGCTGGGTGGTG
GAGGCCCGGAGGCACATCCTGGCCATCCTGCAGGACTGCCCGTCCCTGCGGCCCCCCATC
GACCACCTGTGTGAGCTGCTGCCGCGCCTGCAGGCCCGCTACTACTCCATCGCCTCATCC
TCCAAGGTCCACCCCAACTCTGTGCACATCTGTGCGGTGGTTGTGGAGTACGAGACCAAG
GCCGGCCGCATCAACAAGGGCGTGGCCACCAACTGGCTGCGGGCCAAGGAGCCTGTCGGG
GAGAACGGCGGCCGTGCGCTGGTGCCCATGTTCGTGCGCAAGTCCCAGTTACGCCTGCCC
TTCAAGGCCACCACGCCTGTCATCATGGTGGGCCCCGGCACCGGGTGGCACCCTTTCATA
GGCTTCATCCAGGAGCGGGCCTGGCTGCGACAGCAGGGCAAGGAGGTGGGGGAGACGCTG
CTGTACTACGGCTGCCGCCGCTCGGATGAGGACTACCTGTACCGGGAGGAGCTGGCGCAG
TTCCACAGGGACGGTGCGCTCACCCAGCTCAACGTGGCCTTCTCCCGGGAGCAGTCCCAC
AAGGTCTACGTCCAGCACCTGCTAAAGCAAGACCGAGAGCACCTGTGGAAGTTGATCGAA
GGCGGTGCCCACATCTACGTCTGTGGGGATGCACGGAACATGGCCAGGGATGTGCAGAAC
ACCTTCTACGACATCGTGGCTGAGCTCGGGGCCATGGAGCACGCGCAGGCGGTGGACTAC
ATCAAGAAACTGATGACCAAGGGCCGCTACTCCCTGGACGTGTGGAGCTAG
Enzyme 5 GenBank Gene ID S90469 Link Image
Enzyme 5 GeneCard ID POR Link Image
Enzyme 5 GenAtlas ID POR Link Image
Enzyme 5 HGNC ID HGNC:9208 Link Image
Enzyme 5 Chromosome Location 7
Enzyme 5 Locus 7q11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Shephard EA, Palmer CN, Segall HJ, Phillips IR: Quantification of cytochrome P450 reductase gene expression in human tissues. Arch Biochem Biophys. 1992 Apr;294(1):168-72. [PubMed Link Image]
  2. Haniu M, McManus ME, Birkett DJ, Lee TD, Shively JE: Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. Biochemistry. 1989 Oct 17;28(21):8639-45. [PubMed Link Image]
  3. Zhao Q, Modi S, Smith G, Paine M, McDonagh PD, Wolf CR, Tew D, Lian LY, Roberts GC, Driessen HP: Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Protein Sci. 1999 Feb;8(2):298-306. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5416
Enzyme 6 Name Dihydroorotate dehydrogenase, mitochondrial precursor
Enzyme 6 Synonyms
  1. Dihydroorotate oxidase
  2. DHOdehase
Enzyme 6 Gene Name DHODH
Enzyme 6 Protein Sequence >Dihydroorotate dehydrogenase, mitochondrial precursor
MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVR
FTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSV
TPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVN
LGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQER
DGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSET
GGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTF
WGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR
Enzyme 6 Number of Residues 395
Enzyme 6 Molecular Weight 42868
Enzyme 6 Theoretical pI 10.23
Enzyme 6 GO Classification
Function
  • catalytic activity
  • dihydroorotate dehydrogenase activity
  • dihydroorotate oxidase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
Process
  • 'de novo' pyrimidine base biosynthesis
  • UMP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine base biosynthesis
  • pyrimidine base metabolism
  • pyrimidine nucleoside monophosphate biosynthesis
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
  • pyrimidine ribonucleoside monophosphate biosynthesis
Component
  • cell
  • membrane
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function (S)-dihydroorotate + O(2) = orotate + H(2)O(2)
Enzyme 6 Pathways
Enzyme 6 Reactions
  • (S)-dihydroorotate + O2 = orotate + H2O2
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-25
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 555594 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q02127 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PYRD_HUMAN Link Image
Enzyme 6 PDB ID 1D3H Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1191 bp
AAATTACCGTGGAGACACCTGCAAAAGCGGGCCCAGGATGCTGTGATCATCCTGGGGGGA
GGAGGACTTCTCTTCGCCTCCTACCTGATGGCCACGGGAGATGAGCGTTTCTATGCTGAA
CACCTGATGCCGACTCTGCAGGGGCTGCTGGACCCGGAGTCAGCCCACAGACTGGCTGTT
CGCTTCACCTCCCTGGGGCTCCTTCCACGGGCCAGATTTCAAGACTCTGACATGCTGGAA
GTGAGAGTTCTGGGCCATAAATTCCGAAATCCAGTAGGAATTGCTGCAGGATTTGACAAG
CATGGGGAAGCCGTGGACGGACTTTATAAGATGGGCTTTGGTTTTGTTGAGATAGGAAGT
GTGACTCCAAAACCTCAGGAAGGAAACCCTAGACCCAGAGTCTTCCGCCTCCCTGAGGAC
CAAGCTGTCATTAACAGGTATGGATTTAACAGTCACGGGCTTTCAGTGGTGGAACACAGG
TTACGGGCCAGACAGCAGAAGCAGGCCAAGCTCACAGAAGATGGACTGCCTCTGGGGGTC
AACTTGGGGAAGAACAAGACCTCAGTGGACGCCGCGGAGGACTACGCAGAAGGGGTGCGC
GTACTGGGCCCCCTGGCCGACTACCTGGTGGTGAATGTGTCCAGCCCCAACACTGCCGGG
CTGCGGAGCCTTCAGGGAAAGGCCGAGCTGCGCCGCCTGCTGACCAAGGTGCTGCAGGAG
AGGGATGGCTTGCGGAGAGTGCACAGGCCGGCAGTCCTGGTGAAGATCGCTCCTGACCTC
ACCAGCCAGGATAAGGAGGACATTGCCAGTGTGGTCAAAGAGTTGGGCATCGATGGGCTG
ATTGTTACGAACACCACCGTGAGTCGCCCTGCGGGCCTCCAGGGTGCCCTGCGCTCTGAA
ACAGGAGGGCTGAGTGGGAAGCCCCTCCGGGATTTATCAACTCAAACCATTCGGGAGATG
TATGCACTCACCCAAGGCCGAGTTCCCATAATTGGGGTTGGTGGTGTGAGCAGCGGGCAG
GACGCGCTGGAGAAGATCCGGGCAGGGGCCTCCCTGGTGCAGCTGTACACGGCCCTCACC
TTCTGGGGGCCACCCGTTGTGGGCAAAGTCAAGCGGGAACTGGAGGCCCTTCTGAAAGAG
CAGGGCTTTGGCGGAGTCACAGATGCCATTGGAGCAGATCATCGGAGGTGA
Enzyme 6 GenBank Gene ID M94065 Link Image
Enzyme 6 GeneCard ID DHODH Link Image
Enzyme 6 GenAtlas ID DHODH Link Image
Enzyme 6 HGNC ID HGNC:2867 Link Image
Enzyme 6 Chromosome Location 16
Enzyme 6 Locus 16q22
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Minet M, Dufour ME, Lacroute F: Cloning and sequencing of a human cDNA coding for dihydroorotate dehydrogenase by complementation of the corresponding yeast mutant. Gene. 1992 Nov 16;121(2):393-6. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5418
Enzyme 7 Name NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor
Enzyme 7 Synonyms
  1. NADH-ubiquinone oxidoreductase 51 kDa subunit
  2. Complex I-51kD
  3. CI-51kD
  4. NADH dehydrogenase flavoprotein 1
Enzyme 7 Gene Name NDUFV1
Enzyme 7 Protein Sequence >NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor
MLATRRLLGWSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGSLSRG
DWYKTKEILLKGPDWILGEIKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEG
EPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAG
LIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPT
TVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELI
EKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRS
TDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIE
GHTICALGDGAAWPVQGLIRHFRPELEERMQRFAQQHQARQAAS
Enzyme 7 Number of Residues 464
Enzyme 7 Molecular Weight 50818
Enzyme 7 Theoretical pI 8.29
Enzyme 7 GO Classification
Function
  • FMN binding
  • NAD binding
  • NADH dehydrogenase (ubiquinone) activity
  • binding
  • catalytic activity
  • cation binding
  • cation transporter activity
  • coenzyme binding
  • cofactor binding
  • hydrogen ion transporter activity
  • ion binding
  • ion transporter activity
  • iron ion binding
  • monovalent inorganic cation transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • transition metal ion binding
  • transporter activity
Process
  • ATP synthesis coupled electron transport
  • ATP synthesis coupled electron transport (sensu Eukaryota)
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • mitochondrial electron transport, NADH to ubiquinone
  • physiological process
Component
Enzyme 7 General Function Energy production and conversion
Enzyme 7 Specific Function Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone
Enzyme 7 Pathways
Enzyme 7 Reactions
  • NADH + H+ + acceptor = NAD+ + reduced acceptor
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-18
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3184148 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P49821 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NDUV1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >72 bp
ATGCTGGCAACACGGCGGCTGCTCGGCTGGTCGCTTCCCGCGCGGGTATCTGTGCGTTTC
AGCGGCGACACG
Enzyme 7 GenBank Gene ID Y17379 Link Image
Enzyme 7 GeneCard ID NDUFV1 Link Image
Enzyme 7 GenAtlas ID NDUFV1 Link Image
Enzyme 7 HGNC ID HGNC:7716 Link Image
Enzyme 7 Chromosome Location 11
Enzyme 7 Locus 11q13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Schuelke M, Loeffen J, Mariman E, Smeitink J, van den Heuvel L: Cloning of the human mitochondrial 51 kDa subunit (NDUFV1) reveals a 100% antisense homology of its 3'UTR with the 5'UTR of the gamma-interferon inducible protein (IP-30) precursor: is this a link between mitochondrial myopathy and inflammation? Biochem Biophys Res Commun. 1998 Apr 17;245(2):599-606. [PubMed Link Image]
  2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  3. Spencer SR, Taylor JB, Cowell IG, Xia CL, Pemble SE, Ketterer B: The human mitochondrial NADH: ubiquinone oxidoreductase 51-kDa subunit maps adjacent to the glutathione S-transferase P1-1 gene on chromosome 11q13. Genomics. 1992 Dec;14(4):1116-8. [PubMed Link Image]
  4. Ali ST, Duncan AM, Schappert K, Heng HH, Tsui LC, Chow W, Robinson BH: Chromosomal localization of the human gene encoding the 51-kDa subunit of mitochondrial complex I (NDUFV1) to 11q13. Genomics. 1993 Nov;18(2):435-9. [PubMed Link Image]
  5. Schuelke M, Smeitink J, Mariman E, Loeffen J, Plecko B, Trijbels F, Stockler-Ipsiroglu S, van den Heuvel L: Mutant NDUFV1 subunit of mitochondrial complex I causes leukodystrophy and myoclonic epilepsy. Nat Genet. 1999 Mar;21(3):260-1. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5426
Enzyme 8 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Enzyme 8 Synonyms
  1. E- NPP 3
  2. Phosphodiesterase I/nucleotide pyrophosphatase 3
  3. Phosphodiesterase I beta
  4. PD-Ibeta
  5. CD203c antigen[Includes: Alkaline phosphodiesterase I
  6. NPPase]
Enzyme 8 Gene Name ENPP3
Enzyme 8 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QKKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
Enzyme 8 Number of Residues 875
Enzyme 8 Molecular Weight 100097
Enzyme 8 Theoretical pI 6.55
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD
Enzyme 8 Pathways
Enzyme 8 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-38
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 2465540 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O14638 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ENPP3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2628 bp
ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA
Enzyme 8 GenBank Gene ID AF005632 Link Image
Enzyme 8 GeneCard ID ENPP3 Link Image
Enzyme 8 GenAtlas ID ENPP3 Link Image
Enzyme 8 HGNC ID HGNC:3358 Link Image
Enzyme 8 Chromosome Location 6
Enzyme 8 Locus 6q22
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5658
Enzyme 9 Name Methionine synthase reductase, mitochondrial precursor
Enzyme 9 Synonyms
  1. MSR
Enzyme 9 Gene Name MTRR
Enzyme 9 Protein Sequence >Methionine synthase reductase, mitochondrial precursor
MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASLRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS
Enzyme 9 Number of Residues 725
Enzyme 9 Molecular Weight 80437
Enzyme 9 Theoretical pI 6.47
Enzyme 9 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 9 General Function Inorganic ion transport and metabolism
Enzyme 9 Specific Function Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(I)alamin + NADPH + H+ + 2 S-adenosylLmethionine
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-24
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 6572540 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9UBK8 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name MTRR_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2178 bp
ATGGGCGCTGCGTCAGTGCGCGCTGGCGCAAGGTTGGTGGAAGTCGCGTTGTGCAGTTTC
ACTGTTACATGCCTTGAAGTGATGAGGAGGTTTCTGTTACTATATGCTACACAGCAGGGA
CAGGCAAAGGCCATCGCAGAAGAAATGTGTGAGCAAGCTGTGGTACATGGATTTTCTGCA
GATCTTCACTGTATTAGTGAATCCGATAAGTATGACCTAAAAACCGAAACAGCTCCTCTT
GTTGTTGTGGTTTCTACCACGGGCACCGGAGACCCACCCGACACAGCCCGCAAGTTTGTT
AAGGAAATACAGAACCAAACACTGCCGGTTGATTTCTTTGCTCACCTGCGGTATGGGTTA
CTGGGTCTCGGTGATTCAGAATACACCTACTTTTGCAATGGGGGGAAGATAATTGATAAA
CGACTTCAAGAGCTTGGAGCCCGGCATTTCTATGACACTGGACATGCAGATGACTGTGTA
GGTTTAGAACTTGTGGTTGAGCCGTGGATTGCTGGACTCTGGCCAGCCCTCAGAAAGCAT
TTTAGGTCAAGCAGAGGACAAGAGGAGATAAGTGGCGCACTCCCGGTGGCATCACCTGCA
TCCTTGAGGACAGACCTTGTGAAGTCAGAGCTGCTACACATTGAATCTCAAGTCGAGCTT
CTGAGATTCGATGATTCAGGAAGAAAGGATTCTGAGGTTTTGAAGCAAAATGCAGTGAAC
AGCAACCAATCCAATGTTGTAATTGAAGACTTTGAGTCCTCACTTACCCGTTCGGTACCC
CCACTCTCACAAGCCTCTCTGAATATTCCTGGTTTACCCCCAGAATATTTACAGGTACAT
CTGCAGGAGTCTCTTGGCCAGGAGGAAAGCCAAGTATCTGTGACTTCAGCAGATCCAGTT
TTTCAAGTGCCAATTTCAAAGGCAGTTCAACTTACTACGAATGATGCCATAAAAACCACT
CTGCTGGTAGAATTGGACATTTCAAATACAGACTTTTCCTATCAGCCTGGAGATGCCTTC
AGCGTGATCTGCCCTAACAGTGATTCTGAGGTACAAAGCCTACTCCAAAGACTGCAGCTT
GAAGATAAAAGAGAGCACTGCGTCCTTTTGAAAATAAAGGCAGACACAAAGAAGAAAGGA
GCTACCTTACCCCAGCATATACCTGCGGGATGTTCTCTCCAGTTCATTTTTACCTGGTGT
CTTGAAATCCGAGCAATTCCTAAAAAGGCATTTTTGCGAGCCCTTGTGGACTATACCAGT
GACAGTGCTGAAAAGCGCAGGCTACAGGAGCTGTGCAGTAAACAAGGGGCAGCCGATTAT
AGCCGCTTTGTACGAGATGCCTGTGCCTGCTTGTTGGATCTCCTCCTCGCTTTCCCTTCT
TGCCAGCCACCACTCAGTCTCCTGCTCGAACATCTTCCTAAACTTCAACCCAGACCATAT
TCGTGTGCAAGCTCAAGTTTATTTCACCCAGGAAAGCTCCATTTTGTCTTCAACATTGTG
GAATTTCTGTCTACTGCCACAACAGAGGTTCTGCGGAAGGGAGTATGTACAGGCTGGCTG
GCCTTGTTGGTTGCTTCAGTTCTTCAGCCAAACATACATGCATCCCATGAAGACAGCGGG
AAAGCCCTGGCTCCTAAGATATCCATCTCTCCTCGAACAACAAATTCTTTCCACTTACCA
GATGACCCCTCAATCCCCATCATAATGGTGGGTCCAGGAACCGGCATAGCCCCGTTTATT
GGGTTCCTACAACATAGAGAGAAACTCCAAGAACAACACCCAGATGGAAATTTTGGAGCA
ATGTGGTTGTTTTTTGGCTGCAGGCATAAGGATAGGGATTATCTATTCAGAAAAGAGCTC
AGACATTTCCTTAAGCATGGGATCTTAACTCATCTAAAGGTTTCCTTCTCAAGAGATGCT
CCTGTTGGGGAGGAGGAAGCCCCAGCAAAGTATGTACAAGACAACATCCAGCTTCATGGC
CAGCAGGTGGCGAGAATCCTCCTCCAGGAGAACGGCCATATTTATGTGTGTGGAGATGCA
AAGAATATGGCCAAGGATGTACATGATGCCCTTGTGCAAATAATAAGCAAAGAGGTTGGA
GTTGAAAAACTAGAAGCAATGAAAACCCTGGCCACTTTAAAAGAAGAAAAACGCTACCTT
CAGGATATTTGGTCATAA
Enzyme 9 GenBank Gene ID AF121213 Link Image
Enzyme 9 GeneCard ID MTRR Link Image
Enzyme 9 GenAtlas ID MTRR Link Image
Enzyme 9 HGNC ID HGNC:7473 Link Image
Enzyme 9 Chromosome Location 5
Enzyme 9 Locus 5p15.3-p15.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Leclerc D, Odievre M, Wu Q, Wilson A, Huizenga JJ, Rozen R, Scherer SW, Gravel RA: Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene. Gene. 1999 Nov 15;240(1):75-88. [PubMed Link Image]
  2. Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA: Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):3059-64. [PubMed Link Image]
  3. Wilson A, Leclerc D, Rosenblatt DS, Gravel RA: Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. Hum Mol Genet. 1999 Oct;8(11):2009-16. [PubMed Link Image]
  4. Wilson A, Platt R, Wu Q, Leclerc D, Christensen B, Yang H, Gravel RA, Rozen R: A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida. Mol Genet Metab. 1999 Aug;67(4):317-23. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5947
Enzyme 10 Name Pyridoxine-5'-phosphate oxidase
Enzyme 10 Synonyms
  1. Pyridoxamine-phosphate oxidase
Enzyme 10 Gene Name PNPO
Enzyme 10 Protein Sequence >Pyridoxine-5'-phosphate oxidase
MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVK
QFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKE
LDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPD
REYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGD
SPLGPMTHRGEEDWLYERLAP
Enzyme 10 Number of Residues 261
Enzyme 10 Molecular Weight 29988
Enzyme 10 Theoretical pI 7.09
Enzyme 10 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • pyridoxamine-phosphate oxidase activity
Process
  • cellular metabolism
  • metabolism
  • physiological process
  • pyridoxine biosynthesis
  • pyridoxine metabolism
  • vitamin B6 metabolism
  • vitamin metabolism
  • water-soluble vitamin metabolism
Component
Enzyme 10 General Function Coenzyme transport and metabolism
Enzyme 10 Specific Function Oxidizes PNP and PMP into pyridoxal 5'-phosphate (PLP)
Enzyme 10 Pathways
Enzyme 10 Reactions
  • pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + ammonia + H2O2
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 21728336 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9NVS9 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PNPO_HUMAN Link Image
Enzyme 10 PDB ID 1NRG Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >786 bp
ATGACGTGCTGGCTGCGGGGCGTCACGGCGACGTTCGGGCGACCTGCCGAGTGGCCAGGC
TACCTCAGTCACCTGTGTGGTCGCAGTGCTGCCATGGACCTGGGACCCATGCGCAAGAGT
TACCGCGGGGACCGAGAGGCATTTGAGGAGACTCATCTGACCTCCCTTGACCCAGTGAAA
CAGTTTGCTGCCTGGTTTGAGGAGGCTGTTCAGTGTCCTGACATAGGGGAAGCCAATGCC
ATGTGTCTGGCTACCTGCACCAGAGATGGAAAACCCTCTGCTCGCATGTTGCTGCTGAAG
GGCTTCGGGAAAGATGGCTTCCGCTTCTTCACTAACTTCGAGAGTCGAAAAGGAAAAGAG
CTGGACTCTAATCCCTTTGCTTCCCTTGTCTTCTACTGGGAGCCACTTAACCGTCAGGTG
CGTGTGGAAGGCCCTGTGAAGAAACTGCCTGAGGAGGAGGCTGAGTGCTACTTCCACTCC
CGCCCCAAGAGCAGCCAGATTGGGGCTGTGGTCAGCCACCAGAGTTCTGTGATCCCTGAT
CGGGAGTATCTGAGAAAGAAAAATGAGGAACTGGAACAGCTCTACCAGGATCAAGAGGTG
CCCAAGCCAAAATCCTGGGGTGGCTATGTCCTGTACCCTCAGGTGATGGAGTTCTGGCAA
GGTCAAACCAACCGCCTGCATGACCGGATAGTCTTTCGGCGGGGCCTACCCACAGGAGAT
TCCCCTTTGGGGCCCATGACCCACCGCGGGGAGGAAGACTGGCTCTATGAGAGACTTGCA
CCTTAA
Enzyme 10 GenBank Gene ID AF468030 Link Image
Enzyme 10 GeneCard ID PNPO Link Image
Enzyme 10 GenAtlas ID PNPO Link Image
Enzyme 10 HGNC ID HGNC:30260 Link Image
Enzyme 10 Chromosome Location 17
Enzyme 10 Locus 17q21.32
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK: Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. Protein Sci. 2003 Jul;12(7):1455-63. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6002
Enzyme 11 Name Dihydropyrimidine dehydrogenase [NADP+] precursor
Enzyme 11 Synonyms
  1. DPD
  2. DHPDHase
  3. Dihydrouracil dehydrogenase
  4. Dihydrothymine dehydrogenase
Enzyme 11 Gene Name DPYD
Enzyme 11 Protein Sequence >Dihydropyrimidine dehydrogenase [NADP+] precursor
MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFD
DIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDN
PLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPE
KMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDV
VNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQD
QGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVF
IVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWN
EDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGG
DVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGL
KFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMY
GPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDS
GADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSI
ARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTS
IARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYL
KSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQ
NVAFSPLKRSCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCY
MTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLS
VNPVC
Enzyme 11 Number of Residues 1025
Enzyme 11 Molecular Weight 111375
Enzyme 11 Theoretical pI 7.05
Enzyme 11 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • dihydroorotate dehydrogenase activity
  • dihydroorotate oxidase activity
  • disulfide oxidoreductase activity
  • electron transporter activity
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • transition metal ion binding
  • transporter activity
Process
  • 'de novo' pyrimidine base biosynthesis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base biosynthesis
  • pyrimidine base metabolism
Component
  • cell
  • cytoplasm
  • intracellular
  • membrane
Enzyme 11 General Function Amino acid transport and metabolism
Enzyme 11 Specific Function Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil
Enzyme 11 Pathways
Enzyme 11 Reactions
  • 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 558305 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q12882 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name DPYD_HUMAN Link Image
Enzyme 11 PDB ID 1GTE Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >3078 bp
ATGGCCCCTGTGCTCAGTAAGGACTCGGCGGACATCGAGAGTATCCTGGCTTTAAATCCT
CGAACACAAACTCATGCAACTCTGTGTTCCACTTCGGCCAAGAAATTAGACAAGAAACAT
TGGAAAAGAAATCCTGATAAGAACTGCTTTAATTGTGAGAAGCTGGAGAATAATTTTGAT
GACATCAAGCACACGACTCTTGGTGAGCGAGGAGCTCTCCGAGAAGCAATGAGATGCCTG
AAATGTGCAGATGCCCCGTGTCAGAAGAGCTGTCCAACTAATCTTGATATTAAATCATTC
ATCACAAGTATTGCAAACAAGAACTATTATGGAGCTGCTAAGATGATATTTTCTGACAAC
CCACTTGGTCTGACTTGTGGAATGGTATGTCCAACCTCTGATCTATGTGTAGGTGGATGC
AATTTATATGCCACTGAAGAGGGACCCATTAATATTGGTGGATTGCAGCAATTTGCTACT
GAGGTATTCAAAGCAATGAGTATCCCACAGATCAGAAATCCTTCGCTGCCTCCCCCAGAA
AAAATGTCTGAAGCCTATTCTGCAAAGATTGCTCTTTTTGGTGCTGGGCCTGCAAGTATA
AGTTGTGCTTCCTTTTTGGCTCGATTGGGGTACTCTGACATCACTATATTTGAAAAACAA
GAATATGTTGGTGGTTTAAGTACTTCTGAAATTCCTCAGTTCCGGCTGCCGTATGATGTA
GTGAATTTTGAGATTGAGCTAATGAAGGACCTTGGTGTAAAGATAATTTGCGGTAAAAGC
CTTTCAGTGAATGAAATGACTCTTAGCACTTTGAAAGAAAAAGGCTACAAAGCTGCTTTC
ATTGGAATAGGTTTGCCAGAACCCAATAAAGATGCCATCTTCCAAGGCCTGACGCAGGAC
CAGGGGTTTTATACATCCAAAGACTTTTTGCCACTTGTAGCCAAAGGCAGTAAAGCAGGA
ATGTGCGCCTGTCACTCTCCATTGCCATCGATACGGGGAGTCGTGATTGTACTTGGAGCT
GGAGACACTGCCTTCGACTGTGCAACATCTGCTCTACGTTGTGGAGCTCGCCGAGTGTTC
ATCGTCTTCAGAAAAGGCTTTGTTAATATAAGAGCTGTCCCTGAGGAGATGGAGCTTGCT
AAGGAAGAAAAGTGTGAATTTCTGCCATTCCTGTCCCCACGGAAGGTTATAGTAAAAGGT
GGGAGAATTGTTGCTATGCAGTTTGTTCGGACAGAGCAAGATGAAACTGGAAAATGGAAT
GAAGATGAAGATCAGATGGTCCATCTGAAAGCCGATGTGGTCATCAGTGCCTTTGGTTCA
GTTCTGAGTGATCCTAAAGTAAAAGAAGCCTTGAGCCCTATAAAATTTAACAGATGGGGT
CTCCCAGAAGTAGATCCAGAAACTATGCAAACTAGTGAAGCATGGGTATTTGCAGGTGGT
GATGTCGTTGGTTTGGCTAACACTACAGTGGAATCGGTGAATGATGGAAAGCAAGCTTCT
TGGTACATTCACAAATACGTACAGTCACAATATGGAGCTTCCGTTTCTGCCAAGCCTGAA
CTACCCCTCTTTTACACTCCTATTGATCTGGTGGACATTAGTGTAGAAATGGCCGGATTG
AAGTTTATAAATCCTTTTGGTCTTGCTAGCGCAACTCCAGCCACCAGCACATCAATGATT
CGAAGAGCTTTTGAAGCTGGATGGGGTTTTGCCCTCACCAAAACTTTCTCTCTTGATAAG
GACATTGTGACAAATGTTTCCCCCAGAATCATCCGGGGAACCACCTCTGGCCCCATGTAT
GGCCCTGGACAAAGCTCCTTTCTGAATATTGAGCTCATCAGTGAGAAAACGGCTGCATAT
TGGTGTCAAAGTGTCACTGAACTAAAGGCTGACTTCCCAGACAACATTGTGATTGCTAGC
ATTATGTGCAGTTACAATAAAAATGACTGGACGGAACTTGCCAAGAAGTCTGAGGATTCT
GGAGCAGATGCCCTGGAGTTAAATTTATCATGTCCACATGGCATGGGAGAAAGAGGAATG
GGCCTGGCCTGTGGGCAGGATCCAGAGCTGGTGCGGAACATCTGCCGCTGGGTTAGGCAA
GCTGTTCAGATTCCTTTTTTTGCCAAGCTGACCCCAAATGTCACTGATATTGTGAGCATC
GCAAGAGCTGCAAAGGAAGGTGGTGCCAATGGCGTTACAGCCACCAACACTGTCTCAGGT
CTGATGGGATTAAAATCTGATGGCACACCTTGGCCAGCAGTGGGGATTGCAAAGCGAACT
ACATATGGAGGAGTGTCTGGGACAGCAATCAGACCTATTGCTTTGAGAGCTGTGACCTCC
ATTGCTCGTGCTCTGCCTGGATTTCCCATTTTGGCTACTGGTGGAATTGACTCTGCTGAA
AGTGGTCTTCAGTTTCTCCATAGTGGTGCTTCCGTCCTCCAGGTATGCAGTGCCATTCAG
AATCAGGATTTCACTGTGATCGAAGACTACTGCACTGGCCTCAAAGCCCTGCTTTATCTG
AAAAGCATTGAAGAACTACAAGACTGGGATGGACAGAGTCCAGCTACTGTGAGTCACCAG
AAAGGGAAACCAGTTCCACGTATAGCTGAACTCATGGACAAGAAACTGCCAAGTTTTGGA
CCTTATCTGGAACAGCGCAAGAAAATCATAGCAGAAAACAAGATTAGACTGAAAGAACAA
AATGTAGCTTTTTCACCACTTAAGAGAAGCTGTTTTATCCCCAAAAGGCCTATTCCTACC
ATCAAGGATGTAATAGGAAAAGCACTGCAGTACCTTGGAACATTTGGTGAATTGAGCAAC
GTAGAGCAAGTTGTGGCTATGATTGATGAAGAAATGTGTATCAACTGTGGTAAATGCTAC
ATGACCTGTAATGATTCTGGCTACCAGGCTATACAGTTTGATCCAGAAACCCACCTGCCC
ACCATAACCGACACTTGTACAGGCTGTACTCTGTGTCTCAGTGTTTGCCCTATTGTCGAC
TGCATCAAAATGGTTTCCAGGACAACACCTTATGAACCAAAGAGAGGCGTACCCTTATCT
GTGAATCCGGTGTGTTAA
Enzyme 11 GenBank Gene ID U09178 Link Image
Enzyme 11 GeneCard ID DPYD Link Image
Enzyme 11 GenAtlas ID DPYD Link Image
Enzyme 11 HGNC ID HGNC:3012 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1p22
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Yokota H, Fernandez-Salguero P, Furuya H, Lin K, McBride OW, Podschun B, Schnackerz KD, Gonzalez FJ: cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria. J Biol Chem. 1994 Sep 16;269(37):23192-6. [PubMed Link Image]
  2. Johnson MR, Wang K, Tillmanns S, Albin N, Diasio RB: Structural organization of the human dihydropyrimidine dehydrogenase gene. Cancer Res. 1997 May 1;57(9):1660-3. [PubMed Link Image]
  3. Ogura K, Nishiyama T, Takubo H, Kato A, Okuda H, Arakawa K, Fukushima M, Nagayama S, Kawaguchi Y, Watabe T: Suicidal inactivation of human dihydropyrimidine dehydrogenase by (E)-5-(2-bromovinyl)uracil derived from the antiviral, sorivudine. Cancer Lett. 1998 Jan 9;122(1-2):107-13. [PubMed Link Image]
  4. Vreken P, Van Kuilenburg AB, Meinsma R, Smit GP, Bakker HD, De Abreu RA, van Gennip AH: A point mutation in an invariant splice donor site leads to exon skipping in two unrelated Dutch patients with dihydropyrimidine dehydrogenase deficiency. J Inherit Metab Dis. 1996;19(5):645-54. [PubMed Link Image]
  5. Fernandez-Salguero PM, Sapone A, Wei X, Holt JR, Jones S, Idle JR, Gonzalez FJ: Lack of correlation between phenotype and genotype for the polymorphically expressed dihydropyrimidine dehydrogenase in a family of Pakistani origin. Pharmacogenetics. 1997 Apr;7(2):161-3. [PubMed Link Image]
  6. Lu ZH, Zhang R, Diasio RB: Purification and characterization of dihydropyrimidine dehydrogenase from human liver. J Biol Chem. 1992 Aug 25;267(24):17102-9. [PubMed Link Image]
  7. Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Dihydropyrimidine dehydrogenase (DPD) deficiency: identification and expression of missense mutations C29R, R886H and R235W. Hum Genet. 1997 Dec;101(3):333-8. [PubMed Link Image]
  8. Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Identification of novel point mutations in the dihydropyrimidine dehydrogenase gene. J Inherit Metab Dis. 1997 Jul;20(3):335-8. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6067
Enzyme 12 Name Hydroxyacid oxidase 1
Enzyme 12 Synonyms
  1. HAOX1
  2. Glycolate oxidase
  3. GOX
Enzyme 12 Gene Name HAO1
Enzyme 12 Protein Sequence >Hydroxyacid oxidase 1
MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET
DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE
AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ
LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR
GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV
LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV
RKNPLAVSKI
Enzyme 12 Number of Residues 370
Enzyme 12 Molecular Weight 40925
Enzyme 12 Theoretical pI 8.29
Enzyme 12 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 12 General Function Energy production and conversion
Enzyme 12 Specific Function Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids
Enzyme 12 Pathways
  • Glyoxylate and Dicarboxylate Metabolism (map00630 Link Image)
Enzyme 12 Reactions
  • (S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 7530485 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9UJM8 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name HAOX1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1113 bp
ATGCTCCCCCGGCTAATTTGTATCAATGATTATGAACAACATGCTAAATCAGTACTTCCA
AAGTCTATATATGACTATTACAGGTCTGGGGCAAATGATGAAGAAACTTTGGCTGATAAT
ATTGCAGCATTTTCCAGATGGAAGCTGTATCCAAGGATGCTCCGGAATGTTGCTGAAACA
GATCTGTCGACTTCTGTTTTAGGACAGAGGGTCAGCATGCCAATATGTGTGGGGGCTACG
GCCATGCAGCGCATGGCTCATGTGGACGGCGAGCTTGCCACTGTGAGAGCCTGTCAGTCC
CTGGGAACGGGCATGATGTTGAGTTCCTGGGCCACCTCCTCAATTGAAGAAGTGGCGGAA
GCTGGTCCTGAGGCACTTCGTTGGCTGCAACTGTATATCTACAAGGACCGAGAAGTCACC
AAGAAGCTAGTGCGGCAGGCAGAGAAGATGGGCTACAAGGCCATATTTGTGACAGTGGAC
ACACCTTACCTGGGCAACCGTCTGGATGATGTGCGTAACAGATTCAAACTGCCGCCACAA
CTCAGGATGAAAAATTTTGAAACCAGTACTTTATCATTTTCTCCTGAGGAAAATTTTGGA
GACGACAGTGGACTTGCTGCATATGTGGCTAAAGCAATAGACCCATCTATCAGCTGGGAA
GATATCAAATGGCTGAGAAGACTGACATCATTGCCAATTGTTGCAAAGGGCATTTTGAGA
GGTGATGATGCCAGGGAGGCTGTTAAACATGGCTTGAATGGGATCTTGGTGTCGAATCAT
GGGGCTCGACAACTCGATGGGGTGCCAGCCACTATTGATGTTCTGCCAGAAATTGTGGAG
GCTGTGGAAGGGAAGGTGGAAGTCTTCCTGGACGGGGGTGTGCGGAAAGGCACTGATGTT
CTGAAAGCTCTGGCTCTTGGCGCCAAGGCTGTGTTTGTGGGGAGACCAATCGTTTGGGGC
TTAGCTTTCCAGGGGGAGAAAGGTGTTCAAGATGTCCTCGAGATACTAAAGGAAGAATTC
CGGTTGGCCATGGCTCTGAGTGGGTGCCAGAATGTGAAAGTCATCGACAAGACATTGGTG
AGGAAAAATCCTTTGGCCGTTTCCAAGATCTGA
Enzyme 12 GenBank Gene ID AF244134 Link Image
Enzyme 12 GeneCard ID HAO1 Link Image
Enzyme 12 GenAtlas ID HAO1 Link Image
Enzyme 12 HGNC ID HGNC:4809 Link Image
Enzyme 12 Chromosome Location 20
Enzyme 12 Locus 20p12
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Williams E, Cregeen D, Rumsby G: Identification and expression of a cDNA for human glycolate oxidase. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):246-8. [PubMed Link Image]
  2. Jones JM, Morrell JC, Gould SJ: Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J Biol Chem. 2000 Apr 28;275(17):12590-7. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6068
Enzyme 13 Name Hydroxyacid oxidase 2
Enzyme 13 Synonyms
  1. HAOX2
  2. (S-2-hydroxy-acid oxidase, peroxisomal
  3. Long chain alpha-hydroxy acid oxidase
  4. Long- chain L-2-hydroxy acid oxidase
Enzyme 13 Gene Name HAO2
Enzyme 13 Protein Sequence >Hydroxyacid oxidase 2
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDT
RTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAA
PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLT
DLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQG
IIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG
RPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
Enzyme 13 Number of Residues 351
Enzyme 13 Molecular Weight 38839
Enzyme 13 Theoretical pI 7.69
Enzyme 13 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 13 General Function Energy production and conversion
Enzyme 13 Specific Function Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids
Enzyme 13 Pathways
  • Glyoxylate and Dicarboxylate Metabolism (map00630 Link Image)
Enzyme 13 Reactions
  • (S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 7208438 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9NYQ3 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name HAOX2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1056 bp
ATGTCCTTGGTGTGTTTGACAGACTTTCAGGCCCATGCGCGAGAGCAGCTGTCTAAGTCA
ACTCGGGATTTTATTGAAGGTGGAGCAGATGACAGCATCACGCGGGATGACAACATTGCA
GCATTTAAAAGAATTCGCCTCCGTCCGCGGTACCTGAGAGATGTGTCTGAGGTGGACACC
AGAACCACAATCCAAGGGGAGGAGATCAGTGCCCCTATTTGTATCGCACCCACAGGGTTC
CACTGCCTTGTCTGGCCTGATGGGGAAATGAGCACAGCAAGAGCTGCCCAAGCGGCTGGT
ATCTGCTACATCACCAGCACATTTGCCAGCTGTAGCCTTGAAGACATTGTCATTGCAGCT
CCCGAAGGCCTCCGATGGTTCCAACTCTATGTGCATCCAGACCTGCAGCTGAACAAACAG
TTGATCCAGAGGGTAGAATCCCTAGGTTTCAAAGCTTTGGTAATAACTTTGGATACACCT
GTATGTGGCAACAGGCGACATGACATTCGAAACCAGTTGAGGAGGAACTTAACACTAACA
GATCTTCAATCACCTAAAAAGGGAAATGCAATACCTTATTTCCAGATGACTCCTATCAGC
ACTTCTCTCTGCTGGAATGATCTCTCCTGGTTTCAGAGCATAACTCGATTGCCCATCATC
CTGAAAGGGATTTTGACAAAAGAGGATGCAGAGTTAGCTGTGAAGCACAATGTCCAGGGT
ATCATTGTTTCCAACCATGGTGGGAGGCAGCTTGATGAGGTTCTTGCTTCAATTGATGCT
TTGACAGAAGTGGTGGCTGCTGTAAAGGGGAAAATTGAAGTCTACCTGGATGGCGGGGTC
CGAACTGGCAATGATGTGCTGAAGGCTCTGGCCCTTGGAGCTAAGTGCATTTTTCTTGGG
AGACCAATCCTATGGGGCCTTGCCTGCAAGGGTGAACATGGTGTTAAGGAAGTTTTGAAC
ATTTTAACAAATGAGTTCCACACTTCCATGGCCCTTACAGGCTGCCGGTCGGTCGCTGAG
ATCAATCGAAACTTGGTCCAGTTTTCCAGGCTGTAA
Enzyme 13 GenBank Gene ID AF231917 Link Image
Enzyme 13 GeneCard ID HAO2 Link Image
Enzyme 13 GenAtlas ID HAO2 Link Image
Enzyme 13 HGNC ID HGNC:4810 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1p13.3-p13.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Jones JM, Morrell JC, Gould SJ: Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J Biol Chem. 2000 Apr 28;275(17):12590-7. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6214
Enzyme 14 Name Nitric oxide synthase, inducible
Enzyme 14 Synonyms
  1. NOS type II
  2. Inducible NO synthase
  3. Inducible NOS
  4. iNOS
  5. Hepatocyte NOS
  6. HEP- NOS
Enzyme 14 Gene Name NOS2A
Enzyme 14 Protein Sequence >Nitric oxide synthase, inducible
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
Enzyme 14 Number of Residues 1153
Enzyme 14 Molecular Weight 131119
Enzyme 14 Theoretical pI 8.01
Enzyme 14 GO Classification
Function
  • FAD binding
  • FMN binding
  • NADP binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • coenzyme binding
  • cofactor binding
  • electron transporter activity
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleotide binding
  • tetrapyrrole binding
  • transition metal ion binding
  • transporter activity
Process
  • biosynthesis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • nitric oxide biosynthesis
  • physiological process
Component
Enzyme 14 General Function Inorganic ion transport and metabolism
Enzyme 14 Specific Function Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions
Enzyme 14 Pathways
Enzyme 14 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 292242 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P35228 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name NOS2A_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >3462 bp
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGATCCATAGTTTTCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGACCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTCCCCGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCGGAGATGGCCAGGGTCCCCTGCAC
CACGGTGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGCCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGTGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTCGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
Enzyme 14 GenBank Gene ID L09210 Link Image
Enzyme 14 GeneCard ID NOS2A Link Image
Enzyme 14 GenAtlas ID NOS2A Link Image
Enzyme 14 HGNC ID HGNC:7873 Link Image
Enzyme 14 Chromosome Location 17
Enzyme 14 Locus 17q11.2-q12
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR: Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3491-5. [PubMed Link Image]
  2. Sherman PA, Laubach VE, Reep BR, Wood ER: Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. Biochemistry. 1993 Nov 2;32(43):11600-5. [PubMed Link Image]
  3. Charles IG, Palmer RM, Hickery MS, Bayliss MT, Chubb AP, Hall VS, Moss DW, Moncada S: Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11419-23. [PubMed Link Image]
  4. Maier R, Bilbe G, Rediske J, Lotz M: Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. Biochim Biophys Acta. 1994 Sep 21;1208(1):145-50. [PubMed Link Image]
  5. Park CS, Pardhasaradhi K, Gianotti C, Villegas E, Krishna G: Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA. Biochem Biophys Res Commun. 1994 Nov 30;205(1):85-91. [PubMed Link Image]
  6. Hokari A, Zeniya M, Esumi H: Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. J Biochem (Tokyo). 1994 Sep;116(3):575-81. [PubMed Link Image]
  7. Guo FH, De Raeve HR, Rice TW, Stuehr DJ, Thunnissen FB, Erzurum SC: Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7809-13. [PubMed Link Image]
  8. Luss H, Li RK, Shapiro RA, Tzeng E, McGowan FX, Yoneyama T, Hatakeyama K, Geller DA, Mickle DA, Simmons RL, Billiar TR: Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS. J Mol Cell Cardiol. 1997 Apr;29(4):1153-65. [PubMed Link Image]
  9. McLay JS, Chatterjee P, Nicolson AG, Jardine AG, McKay NG, Ralston SH, Grabowski P, Haites NE, MacLeod AM, Hawksworth GM: Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism? Kidney Int. 1994 Oct;46(4):1043-9. [PubMed Link Image]
  10. Bloch KD, Wolfram JR, Brown DM, Roberts JD Jr, Zapol DG, Lepore JJ, Filippov G, Thomas JE, Jacob HJ, Bloch DB: Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17. Genomics. 1995 Jun 10;27(3):526-30. [PubMed Link Image]
  11. Taylor BS, Alarcon LH, Billiar TR: Inducible nitric oxide synthase in the liver: regulation and function. Biochemistry (Mosc). 1998 Jul;63(7):766-81. [PubMed Link Image]
  12. Glynne PA, Darling KE, Picot J, Evans TJ: Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem. 2002 Sep 6;277(36):33132-8. Epub 2002 Jun 21. [PubMed Link Image]
  13. Li H, Raman CS, Glaser CB, Blasko E, Young TA, Parkinson JF, Whitlow M, Poulos TL: Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. J Biol Chem. 1999 Jul 23;274(30):21276-84. [PubMed Link Image]
  14. Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6216
Enzyme 15 Name Nitric-oxide synthase, brain
Enzyme 15 Synonyms
  1. NOS type I
  2. Neuronal NOS
  3. N-NOS
  4. nNOS
  5. Constitutive NOS
  6. NC-NOS
  7. bNOS
Enzyme 15 Gene Name NOS1
Enzyme 15 Protein Sequence >Nitric-oxide synthase, brain
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
Enzyme 15 Number of Residues 1434
Enzyme 15 Molecular Weight 160972
Enzyme 15 Theoretical pI 7.44
Enzyme 15 GO Classification
Function
  • FAD binding
  • FMN binding
  • NADP binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • coenzyme binding
  • cofactor binding
  • electron transporter activity
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleotide binding
  • tetrapyrrole binding
  • transition metal ion binding
  • transporter activity
Process
  • biosynthesis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • nitric oxide biosynthesis
  • physiological process
Component
Enzyme 15 General Function Inorganic ion transport and metabolism
Enzyme 15 Specific Function Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter
Enzyme 15 Pathways
Enzyme 15 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 642526 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P29475 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name NOS1_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >4305 bp
ATGGAGGATCACATGTTCGGTGTTCAGCAAATCCAGCCCAATGTCATTTCTGTTCGTCTC
TTCAAGCGCAAAGTTGGGGGCCTGGGATTTCTGGTGAAGGAGCGGGTCAGTAAGCCGCCC
GTGATCATCTCTGACCTGATTCGTGGGGGCGCCGCAGAGCAGAGTGGCCTCATCCAGGCC
GGAGACATCATTCTTGCGGTCAACGGCCGGCCCTTGGTGGACCTGAGCTATGACAGCGCC
CTGGAGGTACTCAGAGGCATTGCCTCTGAGACCCACGTGGTCCTCATTCTGAGGGGCCCT
GAAGGTTTCACCACGCACCTGGAGACCACCTTTACAGGTGATGGGACCCCCAAGACCATC
CGGGTGACACAGCCCCTGGGTCCCCCCACCAAAGCCGTGGATCTGTCCCACCAGCCACCG
GCCGGCAAAGAACAGCCCCTGGCAGTGGATGGGGCCTCGGGTCCCGGGAATGGGCCTCAG
CATGCCTACGATGATGGGCAGGAGGCTGGCTCACTCCCCCATGCCAACGGCCTGGCCCCC
AGGCCCCCAGGCCAGGACCCCGCGAAGAAAGCAACCAGAGTCAGCCTCCAAGGCAGAGGG
GAGAACAATGAACTGCTCAAGGAGATAGAGCCTGTGCTGAGCCTTCTCACCAGTGGGAGC
AGAGGGGTCAAGGGAGGGGCACCTGCCAAGGCAGAGATGAAAGATATGGGAATCCAGGTG
GACAGAGATTTGGACGGCAAGTCACACAAACCTCTGCCCCTCGGCGTGGAGAACGACCGA
GTCTTCAATGACCTATGGGGGAAGGGCAATGTGCCTGTCGTCCTCAACAACCCATATTCA
GAGAAGGAGCAGCCCCCCACCTCAGGAAAACAGTCCCCCACAAAGAATGGCAGCCCCTCC
AAGTGTCCACGCTTCCTCAAGGTCAAGAACTGGGAGACTGAGGTGGTTCTCACTGACACC
CTCCACCTTAAGAGCACATTGGAAACGGGATGCACTGAGTACATCTGCATGGGCTCCATC
ATGCATCCTTCTCAGCATGCAAGGAGGCCTGAAGACGTCCGCACAAAAGGACAGCTCTTC
CCTCTCGCCAAAGAGTTTATTGATCAATACTATTCATCAATTAAAAGATTTGGCTCCAAA
GCCCACATGGAAAGGCTGGAAGAGGTGAACAAAGAGATCGACACCACTAGCACTTACCAG
CTCAAGGACACAGAGCTCATCTATGGGGCCAAGCACGCCTGGCGGAATGCCTCGCGCTGT
GTGGGCAGGATCCAGTGGTCCAAGCTGCAGGTATTCGATGCCCGTGACTGCACCACGGCC
CACGGGATGTTCAACTACATCTGTAACCATGTCAAGTATGCCACCAACAAAGGGAACCTC
AGGTCTGCCATCACCATATTCCCCCAGAGGACAGACGGCAAGCACGACTTCCGAGTCTGG
AACTCCCAGCTCATCCGCTACGCTGGCTACAAGCAGCCTGACGGCTCCACCCTGGGGGAC
CCAGCCAATGTGCAGTTCACAGAGATATGCATACAGCAGGGCTGGAAACCGCCTAGAGGC
CGCTTCGATGTCCTGCCGCTCCTGCTTCAGGCCAACGGCAATGACCCTGAGCTCTTCCAG
ATTCCTCCAGAGCTGGTGTTGGAAGTTCCCATCAGGCACCCCAAGTTTGAGTGGTTCAAG
GACCTGGGGCTGAAGTGGTACGGCCTCCCCGCCGTGTCCAACATGCTCCTAGAGATTGGC
GGCCTGGAGTTCAGCGCCTGTCCCTTCAGTGGCTGGTACATGGGCACAGAGATTGGTGTC
CGCGACTACTGTGACAACTCCCGCTACAATATCCTGGAGGAAGTGGCCAAGAAGATGAAC
TTAGACATGAGGAAGACGTCCTCCCTGTGGAAGGACCAGGCGCTGGTGGAGATCAATATC
GCGGTTCTCTATAGCTTCCAGAGTGACAAAGTGACCATTGTTGACCATCACTCCGCCACC
GAGTCCTTCATTAAGCACATGGAGAATGAGTACCGCTGCCGGGGGGGCTGCCCTGCCGAC
TGGGTGTGGATCGTGCCCCCCATGTCCGGAAGCATCACCCCTGTGTTCCACCAGGAGATG
CTCAACTACCGGCTCACCCCCTCCTTCGAATACCAGCCTGATCCCTGGAACACGCATGTC
TGGAAAGGCACCAACGGGACCCCCACAAAGCGGCGAGCCATCGGCTTCAAGAAGCTAGCA
GAAGCTGTCAAGTTCTCGGCCAAGCTGATGGGGCAGGCTATGGCCAAGAGGGTGAAAGCG
ACCATCCTCTATGCCACAGAGACAGGCAAATCGCAAGCTTATGCCAAGACCTTGTGTGAG
ATCTTCAAACACGCCTTTGATGCCAAGGTGATGTCCATGGAAGAATATGACATTGTGCAC
CTGGAACATGAAACTCTGGTCCTTGTGGTCACCAGCACCTTTGGCAATGGAGATCCCCCT
GAGAATGGGGAGAAATTCGGCTGTGCTTTGATGGAAATGAGGCACCCCAACTCTGTGCAG
GAAGAAAGGAAGAGCTACAAGGTCCGATTCAACAGCGTCTCCTCCTACTCTGACTCCCAA
AAATCATCAGGCGATGGGCCCGACCTCAGAGACAACTTTGAGAGTGCTGGACCCCTGGCC
AATGTGAGGTTCTCAGTTTTTGGCCTCGGCTCACGAGCATACCCTCACTTTTGCGCCTTC
GGACACGCTGTGGACACCCTCCTGGAAGAACTGGGAGGGGAGAGGATCCTGAAGATGAGG
GAAGGGGATGAGCTCTGTGGGCAGGAAGAGGCTTTCAGGACCTGGGCCAAGAAGGTCTTC
AAGGCAGCCTGTGATGTCTTCTGTGTGGGAGATGATGTCAACATTGAAAAGGCCAACAAT
TCCCTCATCAGCAATGATCGCAGCTGGAAGAGAAACAAGTTCCGCCTCACCTTTGTGGCC
GAAGCTCCAGAACTCACACAAGGTCTATCCAATGTCCACAAAAAGCGAGTCTCAGCTGCC
CGGCTCCTTAGCCGTCAAAACCTCCAGAGCCCTAAATCCAGTCGGTCAACTATCTTCGTG
CGTCTCCACACCAACGGGAGCCAGGAGCTGCAGTACCAGCCTGGGGACCACCTGGGTGTC
TTCCCTGGCAACCACGAGGACCTCGTGAATGCCCTGATCGAGCGGCTGGAGGACGCGCCG
CCTGTCAACCAGATGGTGAAAGTGGAACTGCTGGAGGAGCGGAACACGGCTTTAGGTGTC
ATCAGTAACTGGACAGACGAGCTCCGCCTCCCGCCCTGCACCATCTTCCAGGCCTTCAAG
TACTACCTGGACATCACCACGCCACCAACGCCTCTGCAGCTGCAGCAGTTTGCCTCCCTA
GCTACCAGCGAGAAGGAGAAGCAGCGTCTGCTGGTCCTCAGCAAGGGTTTGCAGGAGTAC
GAGGAATGGAAATGGGGCAAGAACCCCACCATCGTGGAGGTGCTGGAGGAGTTCCCATCT
ATCCAGATGCCGGCCACCCTGCTCCTGACCCAGCTGTCCCTGCTGCAGCCCCGCTACTAT
TCCATCAGCTCCTCCCCAGACATGTACCCTGATGAAGTGCACCTCACTGTGGCCATCGTT
TCCTACCGCACTCGAGATGGAGAAGGACCAATTCACCACGGCGTATGCTCCTCCTGGCTC
AACCGGATACAGGCTGACGAACTGGTCCCCTGTTTCGTGAGAGGAGCACCCAGCTTCCAC
CTGCCCCGGAACCCCCAAGTCCCCTGCATCCTCGTTGGACCAGGCACCGGCATTGCCCCT
TTCCGAAGCTTCTGGCAACAGCGGCAATTTGATATCCAACACAAAGGAATGAACCCCTGC
CCCATGGTCCTGGTCTTCGGGTGCCGGCAATCCAAGATAGATCATATCTACAGGGAAGAG
ACCCTGCAGGCCAAGAACAAGGGGGTCTTCAGAGAGCTGTACACGGCTTACTCCCGGGAG
CCAGACAAACCAAAGAAGTACGTGCAGGACATCCTGCAGGAGCAGCTGGCGGAGTCTGTG
TACCGAGCCCTGAAGGAGCAAGGGGGCCACATATACGTCTGTGGGGACGTCACCATGGCT
GCTGATGTCCTCAAAGCCATCCAGCGCATCATGACCCAGCAGGGGAAGCTCTCGGCAGAG
GACGCCGGCGTATTCATCAGCCGGATGAGGGATGACAACCGATACCATGAGGATATTTTT
GGAGTCACCCTGCGAACGTACGAAGTGACCAACCGCCTTAGATCTGAGTCCATTGCCTTC
ATTGAAGAGAGCAAAAAAGACACCGATGAGGTTTTCAGCTCCTAA
Enzyme 15 GenBank Gene ID U17327 Link Image
Enzyme 15 GeneCard ID NOS1 Link Image
Enzyme 15 GenAtlas ID NOS1 Link Image
Enzyme 15 HGNC ID HGNC:7872 Link Image
Enzyme 15 Chromosome Location 12
Enzyme 15 Locus 12q24.2-q24.31
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Hall AV, Antoniou H, Wang Y, Cheung AH, Arbus AM, Olson SL, Lu WC, Kau CL, Marsden PA: Structural organization of the human neuronal nitric oxide synthase gene (NOS1). J Biol Chem. 1994 Dec 30;269(52):33082-90. [PubMed Link Image]
  2. Fujisawa H, Ogura T, Kurashima Y, Yokoyama T, Yamashita J, Esumi H: Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines. J Neurochem. 1994 Jul;63(1):140-5. [PubMed Link Image]
  3. Nakane M, Schmidt HH, Pollock JS, Forstermann U, Murad F: Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle. FEBS Lett. 1993 Jan 25;316(2):175-80. [PubMed Link Image]
  4. Park CS, Gianotti C, Park R, Krishna G: Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina. Cell Mol Neurobiol. 1996 Aug;16(4):499-515. [PubMed Link Image]
  5. Wang Y, Goligorsky MS, Lin M, Wilcox JN, Marsden PA: A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase. J Biol Chem. 1997 Apr 25;272(17):11392-401. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6217
Enzyme 16 Name Nitric-oxide synthase, endothelial
Enzyme 16 Synonyms
  1. EC-NOS
  2. NOS type III
  3. NOSIII
  4. Endothelial NOS
  5. eNOS
  6. Constitutive NOS
  7. cNOS
Enzyme 16 Gene Name NOS3
Enzyme 16 Protein Sequence >Nitric-oxide synthase, endothelial
MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLT
QPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAP
EQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGD
FRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPP
ELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMST
EIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDH
HAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW
KGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGR
LFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSS
PRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHF
CAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAA
RDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATIL
VRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGP
PPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRY
EEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVL
AYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAP
FRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSRE
PDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELD
EAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDT
NSP
Enzyme 16 Number of Residues 1203
Enzyme 16 Molecular Weight 133290
Enzyme 16 Theoretical pI 7.27
Enzyme 16 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
Process
  • biosynthesis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • nitric oxide biosynthesis
  • physiological process
Component
Enzyme 16 General Function Inorganic ion transport and metabolism
Enzyme 16 Specific Function Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. No mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets
Enzyme 16 Pathways
Enzyme 16 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 189212 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P29474 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name NOS3_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >3612 bp
ATGGGCAACTTGAAGAGCGTGGCCCAGGAGCCTGGGCCACCCTGCGGCCTGGGGCTGGGG
CTGGGCCTTGGGCTGTGCGGCAAGCAGGGCCCAGCCACCCCGGCCCCTGAGCCCAGCCGG
GCCCCAGCATCCCTACTCCCACCAGCGCCAGAACACAGCCCCCCGAGCTCCCCGCTAACC
CAGCCCCCAGAGGGGCCCAAGTTCCCTCGTGTGAAGAACTGGGAGGTGGGGAGCATCACC
TATGACACCCTCAGCGCCCAGGCGCAGCAGGATGGGCCCTGCACCCCAAGACGCTGCCTG
GGCTCCCTGGTATTTCCACGGAAACTACAGGGCCGGCCCTCCCCCGGCCCCCCGGCCCCT
GAGCAGCTGCTGAGTCAGGCCCGGGACTTCATCAACCAGTACTACAGCTCCATTAAGAGG
AGCGGCTCCCAGGCCCACGAACAGCGGCTTCAAGAGGTGGAAGCCGAGGTGGCAGCCACA
GGCACCTACCAGCTTAGGGAGAGCGAGCTGGTGTTCGGGGCTAAGCAGGCCTGGCGCAAC
GCTCCCCGCTGCGTGGGCCGGATCCAGTGGGGGAAGCTGCAGGTGTTCGATGCCCGGGAC
TGCAGGTCTGCACAGGAAATGTTCACCTACATCTGCAACCACATCAAGTATGCCACCAAC
CGGGGCAACCTTCGCTCGGCCATCACAGTGTTCCCGCAGCGCTGCCCTGGCCGAGGAGAC
TTCCGAATCTGGAACAGCCAGCTGGTGCGCTACGCGGGCTACCGGCAGCAGGACGGCTCT
GTGCGGGGGGACCCAGCCAACGTGGAGATCACCGAGCTCTGCATTCAGCACGGCTGGACC
CCAGGAAACGGTCGCTTCGACGTGCTGCCCCTGCTGCTGCAGGCCCCAGATGAGCCCCCA
GAACTCTTCCTTCTGCCCCCCGAGCTGGTCCTTGAGGTGCCCCTGGAGCACCCCACGCTG
GAGTGGTTTGCAGCCCTGGGCCTGCGCTGGTACGCCCTCCCGGCAGTGTCCAACATGCTG
CTGGAAATTGGGGGCCTGGAGTTCCCCGCAGCCCCCTTCAGTGGCTGGTACATGAGCACT
GAGATCGGCACGAGGAACCTGTGTGACCCTCACCGCTACAACATCCTGGAGGATGTGGCT
GTCTGCATGGACCTGGATACCCGGACCACCTCGTCCCTGTGGAAAGACAAGGCAGCAGTG
GAAATCAACGTGGCCGTGCTGCACAGTTACCAGCTAGCCAAAGTCACCATCGTGGACCAC
CACGCCGCCACGGCCTCTTTCATGAAGCACCTGGAGAATGAGCAGAAGGCCAGGGGGGGC
TGCCCTGCAGACTGGGCCTGGATCGTGCCCCCCATCTCGGGCAGCCTCACTCCTGTTTTC
CATCAGGAGATGGTCAACTATTTCCTGTCCCCGGCCTTCCGCTACCAGCCAGACCCCTGG
AAGGGGAGTGCCGCCAAGGGCACCGGCATCACCAGGAAGAAGACCTTTAAAGAAGTGGCC
AACGCCGTGAAGATCTCCGCCTCGCTCATGGGCACGGTGATGGCGAAGCGAGTGAAGGCG
ACAATCCTGTATGGCTCCGAGACCGGCCGGGCCCAGAGCTACGCACAGCAGCTGGGGAGA
CTCTTCCGGAAGGCTTTTGATCCCCGGGTCCTGTGTATGGATGAGTATGACGTGGTGTCC
CTCGAACACGAGACGCTGGTGCTGGTGGTAACCAGCACATTTGGGAATGGGGATCCCCCG
GAGAATGGAGAGAGCTTTGCAGCTGCCCTGATGGAGATGTCCGGCCCCTACAACAGCTCC
CCTCGGCCGGAACAGCACAAGAGTTATAAGATCCGCTTCAACAGCATCTCCTGCTCAGAC
CCACTGGTGTCCTCTTGGCGGCGGAAGAGGAAGGAGTCCAGTAACACAGACAGTGCAGGG
GCCCTGGGCACCCTCAGGTTCTGTGTGTTCGGGCTCGGCTCCCGGGCATACCCCCACTTC
TGCGCCTTTGCTCGTGCCGTGGACACACGGCTGGAGGAACTGGGCGGGGAGCGGCTGCTG
CAGCTGGGCCAGGGCGACGAGCTGTGCGGCCAGGAGGAGGCCTTCCGAGGCTGGGCCCAG
GCTGCCTTCCAGGCCGCCTGTGAGACCTTCTGTGTGGGAGAGGATGCCAAGGCCGCCGCC
CGAGACATCTTCAGCCCCAAACGGAGCTGGAAGCGCCAGAGGTACCGGCTGAGCGCCCAG
GCCGAGGGCCTGCAGTTGCTGCCAGGTCTGATCCACGTGCACAGGCGGAAGATGTTCCAG
GCTACAATCCGCTCAGTGGAAAACCTGCAAAGCAGCAAGTCCACGAGGGCCACCATCCTG
GTGCGCCTGGACACCGGAGGCCAGGAGGGGCTGCAGTACCAGCCGGGGGACCACATAGGT
GTCTGCCCGCCCAACCGGCCCGGCCTTGTGGAGGCGCTGCTGAGCCGCGTGGAGGACCCG
CCGGCGCCCACTGAGCCCGTGGCAGTAGAGCAGCTGGAGAAGGGCAGCCCTGGTGGCCCT
CCCCCCGGCTGGGTGCGGGACCCCCGGCTGCCCCCGTGCACGCTGCGCCAGGCTCTCACC
TTCTTCCTGGACATCACCTCCCCACCCAGCCCTCAGCTCTTGCGGCTGCTCAGCACCTTG
GCAGAAGAGCCCAGGGAACAGCAGGAGCTGGAGGCCCTCAGCCAGGATCCCCGACGCTAC
GAGGAGTGGAAGTGGTTCCGCTGCCCCACGCTGCTGGAGGTGCTGGAGCAGTTCCCGTCG
GTGGCGCTGCCTGCCCCACTGCTCCTCACCCAGCTGCCTCTGCTCCAGCCCCGGTACTAC
TCAGTCAGCTCGGCACCCAGCACCCACCCAGGAGAGATCCACCTCACTGTAGCTGTGCTG
GCATACAGGACTCAGGATGGGCTGGGCCCCCTGCACTATGGAGTCTGCTCCACGTGGCTA
AGCCAGCTCAAGCCCGGAGACCCTGTGCCCTGCTTCATCCGGGGGGCTCCCTCCTTCCGG
CTGCCACCCGATCCCAGCTTGCCCTGCATCCTGGTGGGTCCAGGCACTGGCATTGCCCCC
TTCCGGGGATTCTGGCAGGAGCGGCTGCATGACATTGAGAGCAAAGGGCTGCAGCCCACT
CCCATGACTTTGGTGTTCGGCTGCCGATGCTCCCAACTTGACCATCTCTACCGCGACGAG
GTGCAGAACGCCCAGCAGCGCGGGGTGTTTGGCCGAGTCCTCACCGCCTTCTCCCGGGAA
CCTGACAACCCCAAGACCTACGTGCAGGACATCCTGAGGACGGAGCTGGCTGCGGAGGTG
CACCGCGTGCTGTGCCTCGAGCGGGGCCACATGTTTGTCTGCGGCGATGTTACCATGGCA
ACCAACGTCCTGCAGACCGTGCAGCGCATCCTGGCGACGGAGGGCGACATGGAGCTGGAC
GAGGCCGGCGACGTCATCGGCGTGCTGCGGGATCAGCAACGCTACCACGAAGACATTTTC
GGGCTCACGCTGCGCACCCAGGAGGTGACAAGCCGCATACGCACCCAGAGCTTTTCCTTG
CAGGAGCGTCAGTTGCGGGGCGCAGTGCCCTGGGCGTTCGACCCTCCCGGCTCAGACACC
AACAGCCCCTGA
Enzyme 16 GenBank Gene ID M93718 Link Image
Enzyme 16 GeneCard ID NOS3 Link Image
Enzyme 16 GenAtlas ID NOS3 Link Image
Enzyme 16 HGNC ID HGNC:7876 Link Image
Enzyme 16 Chromosome Location 7
Enzyme 16 Locus 7q36
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Janssens SP, Shimouchi A, Quertermous T, Bloch DB, Bloch KD: Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. J Biol Chem. 1992 Jul 25;267(21):14519-22. [PubMed Link Image]
  2. Marsden PA, Schappert KT, Chen HS, Flowers M, Sundell CL, Wilcox JN, Lamas S, Michel T: Molecular cloning and characterization of human endothelial nitric oxide synthase. FEBS Lett. 1992 Aug 3;307(3):287-93. [PubMed Link Image]
  3. Marsden PA, Heng HH, Scherer SW, Stewart RJ, Hall AV, Shi XM, Tsui LC, Schappert KT: Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene. J Biol Chem. 1993 Aug 15;268(23):17478-88. [PubMed Link Image]
  4. Nadaud S, Bonnardeaux A, Lathrop M, Soubrier F: Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1027-33. [PubMed Link Image]
  5. Miyahara K, Kawamoto T, Sase K, Yui Y, Toda K, Yang LX, Hattori R, Aoyama T, Yamamoto Y, Doi Y, et al.: Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene. Eur J Biochem. 1994 Aug 1;223(3):719-26. [PubMed Link Image]
  6. Robinson LJ, Weremowicz S, Morton CC, Michel T: Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene. Genomics. 1994 Jan 15;19(2):350-7. [PubMed Link Image]
  7. Sase K, Michel T: Expression of constitutive endothelial nitric oxide synthase in human blood platelets. Life Sci. 1995;57(22):2049-55. [PubMed Link Image]
  8. Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed Link Image]
  9. Rosenfeld RJ, Garcin ED, Panda K, Andersson G, Aberg A, Wallace AV, Morris GM, Olson AJ, Stuehr DJ, Tainer JA, Getzoff ED: Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency. Biochemistry. 2002 Nov 26;41(47):13915-25. [PubMed Link Image]
  10. Yoshimura M, Yasue H, Nakayama M, Shimasaki Y, Sumida H, Sugiyama S, Kugiyama K, Ogawa H, Ogawa Y, Saito Y, Miyamoto Y, Nakao K: A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese. Hum Genet. 1998 Jul;103(1):65-9. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6348
Enzyme 17 Name Riboflavin kinase
Enzyme 17 Synonyms
  1. ATP:riboflavin 5'-phosphotransferase
  2. Flavokinase
Enzyme 17 Gene Name RFK
Enzyme 17 Protein Sequence >Riboflavin kinase
MPRADCIMRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASV
GSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLE
SLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH
Enzyme 17 Number of Residues 162
Enzyme 17 Molecular Weight 18410
Enzyme 17 Theoretical pI 8.22
Enzyme 17 GO Classification
Function
  • catalytic activity
  • kinase activity
  • riboflavin kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • physiological process
  • riboflavin and derivative metabolism
  • riboflavin biosynthesis
  • riboflavin metabolism
  • vitamin metabolism
  • water-soluble vitamin metabolism
Component
Enzyme 17 General Function Coenzyme transport and metabolism
Enzyme 17 Specific Function Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN)
Enzyme 17 Pathways
Enzyme 17 Reactions
  • ATP + riboflavin = ADP + FMN
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 7023634 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q969G6 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name RIFK_HUMAN Link Image
Enzyme 17 PDB ID 1Q9S Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >489 bp
ATGCCCCGAGCGGACTGCATTATGAGGCACCTGCCTTACTTCTGCCGGGGTCAAGTGGTG
CGGGGCTTCGGCCGCGGCTCCAAGCAGCTGGGCATCCCCACAGCTAATTTTCCTGAGCAA
GTGGTAGATAATCTTCCAGCTGATATATCCACTGGTATTTACTATGGTTGGGCCAGTGTT
GGAAGTGGAGATGTCCATAAGATGGTGGTGAGCATAGGATGGAACCCATATTACAAGAAT
ACGAAGAAGTCTATGGAAACACATATCATGCATACCTTCAAAGAGGACTTCTATGGGGAA
ATCCTCAGTGTGGCCATTGTTGGCTACCTGAGACCAGAAAAGAACTTTGATTCTTTAGAG
TCACTTATTTCAGCAATTCAAGGTGATATTGAAGAAGCTAAGAAACGACTAGAGTTACCA
GAACATTTGAAAATCAAAGAAGACAATTTCTTCCAGGTTTCTAAAAGCAAAATAATGAAT
GGCCACTGA
Enzyme 17 GenBank Gene ID AK002011 Link Image
Enzyme 17 GeneCard ID RFK Link Image
Enzyme 17 GenAtlas ID RFK Link Image
Enzyme 17 HGNC ID HGNC:30324 Link Image
Enzyme 17 Chromosome Location 9
Enzyme 17 Locus 9q21.13
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Karthikeyan S, Zhou Q, Mseeh F, Grishin NV, Osterman AL, Zhang H: Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch. Structure. 2003 Mar;11(3):265-73. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8658
Enzyme 18 Name Phosphopantothenoylcysteine decarboxylase
Enzyme 18 Synonyms
  1. PPC-DC
  2. CoaC
Enzyme 18 Gene Name PPCDC
Enzyme 18 Protein Sequence >Phosphopantothenoylcysteine decarboxylase
MEPKASCPAAAPLMERKFHVLVGVTGSVAALKLPLLVSKLLDIPGLEVAVVTTERAKHFY
SPQDIPVTLYSDADEWEMWKSRSDPVLHIDLRRWADLLLVAPLDANTLGKVASGICDNLL
TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGA
MAEVGTIVDKVKEVLFQHSGFQQS
Enzyme 18 Number of Residues 204
Enzyme 18 Molecular Weight 22413
Enzyme 18 Theoretical pI 6.01
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Coenzyme transport and metabolism
Enzyme 18 Specific Function Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'- phosphopantotheine
Enzyme 18 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 18 Reactions
  • N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-30
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 10197638 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q96CD2 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name COAC_HUMAN Link Image
Enzyme 18 PDB ID 1QZU Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >384 bp
ATGTGGAAGAGCCGCTCTGACCCAGTTCTGCACATTGACCTGCGGAGGTGGGCAGACCTC
CTGCTGGTGGCTCCTCTTGATGCCAACACTCTGGGGAAGGTGGCCAGTGGCATCTGTGAC
AACTTGCTTACCTGCGTCATGCGGGCCTGGGACCGCAGCAAGCCCCTGCTCTTCTGCCCG
GCCATGAACACCGCCATGTGGGAGCACCCGATCACAGCGCAGCAGGTAGACCAGCTCAAG
GCCTTTGGCTATGTCGAGATCCCCTGTGTGGCCAAGAAGCTGGTGTGCGGAGATGAAGGT
CTCGGGGCCATGGCTGAAGTGGGGACCATCGTGGACAAAGTGAAAGAAGTCCTCTTCCAG
CACAGTGGCTTCCAGCAGAGTTGA
Enzyme 18 GenBank Gene ID AF182419 Link Image
Enzyme 18 GeneCard ID PPCDC Link Image
Enzyme 18 GenAtlas ID PPCDC Link Image
Enzyme 18 HGNC ID HGNC:28107 Link Image
Enzyme 18 Chromosome Location 15
Enzyme 18 Locus 15q24.2
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. 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]
  2. Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A: Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J Biol Chem. 2002 Jun 14;277(24):21431-9. Epub 2002 Mar 28. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 12937
Enzyme 19 Name Lysophosphatidic acid phosphatase type 6 precursor
Enzyme 19 Synonyms
  1. Acid phosphatase 6, lysophosphatidic
  2. Acid phosphatase-like protein 1
  3. PACPL1
Enzyme 19 Gene Name ACP6
Enzyme 19 Protein Sequence >Lysophosphatidic acid phosphatase type 6 precursor
MITGVFSMRLWTPVGVLTSLAYCLHQRRVALAELQEADGQCPVDRSLLKLKMVQVVFRHG
ARSPLKPLPLEEQVEWNPQLLEVPPQTQFDYTVTNLAGGPKPYSPYDSQYHETTLKGGMF
AGQLTKVGMQQMFALGERLRKNYVEDIPFLSPTFNPQEVFIRSTNIFRNLESTRCLLAGL
FQCQKEGPIIIHTDEADSEVLYPNYQSCWSLRQRTRGRRQTASLQPGISEDLKKVKDRMG
IDSSDKVDFFILLDNVAAEQAHNLPSCPMLKRFARMIEQRAVDTSLYILPKEDRESLQMA
VGPFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFDHKWPPFAVDLT
MELYQHLESKEWFVQLYYHGKEQVPRGCPDGLCPLDMFLNAMSVYTLSPEKYHALCSQTQ
VMEVGNEE
Enzyme 19 Number of Residues 428
Enzyme 19 Molecular Weight 48887
Enzyme 19 Theoretical pI 6.44
Enzyme 19 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
Component
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Hydrolyzes lysophosphatidic acid to monoacylglycerol
Enzyme 19 Pathways
Enzyme 19 Reactions
  • a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626] ALL_REAC R00626 > R00548 R03024
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-32
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 6691475 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NPH0 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PPA6_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 AB031478 Link Image
Enzyme 19 GeneCard ID Q9NPH0 Link Image
Enzyme 19 GenAtlas ID ACP6 Link Image
Enzyme 19 HGNC ID HGNC:29609 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Hiroyama M, Takenawa T: Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis. J Biol Chem. 1999 Oct 8;274(41):29172-80. [PubMed Link Image]
  2. Takayama I, Daigo Y, Ward SM, Sanders KM, Walker RL, Horowitz B, Yamanaka T, Fujino MA: Novel human and mouse genes encoding an acid phosphatase family member and its downregulation in W/W(V) mouse jejunum. Gut. 2002 Jun;50(6):790-6. [PubMed Link Image]
  3. 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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 13058
Enzyme 20 Name Growth-inhibiting protein 16
Enzyme 20 Synonyms
  1. Hydroxyacid oxidase 2
  2. Long chain, isoform CRA_b
Enzyme 20 Gene Name GIG16
Enzyme 20 Protein Sequence >Growth-inhibiting protein 16
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDT
RTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAA
PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLT
DLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQG
IIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG
RPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
Enzyme 20 Number of Residues 351
Enzyme 20 Molecular Weight 38839
Enzyme 20 Theoretical pI 7.69
Enzyme 20 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 20 General Function Energy production and conversion
Enzyme 20 Specific Function Not Available
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 46981963 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q2TU86 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name Q2TU86_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 AY513277 Link Image
Enzyme 20 GeneCard ID Q2TU86 Link Image
Enzyme 20 GenAtlas ID GIG16 Link Image
Enzyme 20 HGNC ID HGNC:4810 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References Not Available
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 13102
Enzyme 21 Name FAD synthetase
Enzyme 21 Synonyms
  1. FMN adenylyltransferase
  2. FAD pyrophosphorylase
  3. Flavin adenine dinucleotide synthetase[Includes: Molybdenum cofactor biosynthesis protein-like region
  4. FAD synthetase region]
Enzyme 21 Gene Name FLAD1
Enzyme 21 Protein Sequence >FAD synthetase
MGWDLGTRLFQRQEQRSRLSRIWLEKTRVFLEGSTRTPALPHCLFWLLQVPSTQDPLFPG
YGPQCPVDLAGPPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVTAGIIIVGD
EILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIG
PTHDDVTFEAVAQAFGDELKPHPKLEAATKALGGEGWEKLSLVPSSARLHYGTDPCTGQP
FRFPLVSVRNVYLFPGIPELLRRVLEGMKGLFQNPAVQFHSKELYVAADEASIAPILAEA
QAHFGRRLGLGSYPDWGSNYYQVKLTLDSEEEGPLEECLAYLTARLPQGSLVPYMPNAVE
QASEAVYKLAESGSSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAV
QRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQARHPQ
LEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILY
DRGYTSLGSRENTVRNPALKCLSPGGHPTYRPAYLLENEEEERNSRT
Enzyme 21 Number of Residues 587
Enzyme 21 Molecular Weight 65266
Enzyme 21 Theoretical pI 6.92
Enzyme 21 GO Classification
Function
  • amine binding
  • amino acid binding
  • binding
  • carboxyl- and carbamoyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • Mo-molybdopterin cofactor biosynthesis
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme
Enzyme 21 Pathways
Enzyme 21 Reactions
  • ATP + FMN = diphosphate + FAD [RN:R00161] ALL_REAC R00161
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 91805307 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8NFF5 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name FAD1_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID DQ458779 Link Image
Enzyme 21 GeneCard ID Q8NFF5 Link Image
Enzyme 21 GenAtlas ID FLAD1 Link Image
Enzyme 21 HGNC ID HGNC:24671 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 13990
Enzyme 22 Name NADPH-dependent FMN and FAD containing oxidoreductase
Enzyme 22 Synonyms
  1. NADPH dependent diflavin oxidoreductase 1
  2. cDNA FLJ75288, highly similar to Homo sapiens NADPH dependent diflavin oxidoreductase 1
  3. NDOR1, mRNA
Enzyme 22 Gene Name NR1
Enzyme 22 Protein Sequence >NADPH-dependent FMN and FAD containing oxidoreductase
MPSPQLLVLFGSQTGTAQDVSERLGREARRRRLGCRVQALDSYPVVNLINEPLVIFVCAT
TGQGDPPDNMKNFWRFIFRKNLPSTALCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLG
GSALLPVCLGDDQHELGPDAAVDPWLRDLWDRVLGLYPPPPGLTEIPPGVPLPSKFTLLF
LQEAPSTGSEGQRVAHPGSQEPPSESKPFLAPMISNQRVTGPSHFQDVRLIEFDILGSGI
SFAAGDVVLIQPSNSAAHVQRFCQVLGLDPDQLFMLQPREPDVSSPTRLPQPCSMRHLVS
HYLDIASVPRRSFFELLACLSLHELEREKLLEFSSAQGQEELFEYCNRPRRTILEVLCDF
PHTAAAIPPDYLLDLIPVIRPRAFSIASSLLTHPSRLQILVAVVQFQTRLKEPRRGLCSS
WLASLDPGQGPVRVPLWVRPGSLAFPETPDTPVIMVGPGTGVAPFRAAIQERVAQGQTGN
FLFFGCRWRDQDFYWEAEWQELEKRDCLTLIPAFSREQEQKVYVQHRLRELGSLVWELLD
RQGAYFYLAGNAKSMPADVSEALMSIFQEEGGLCSPDAAAYLARLQQTRRFQTETWA
Enzyme 22 Number of Residues 597
Enzyme 22 Molecular Weight 66763
Enzyme 22 Theoretical pI 6.30
Enzyme 22 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • electron transporter activity
  • nucleotide binding
  • oxidoreductase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 22 General Function Inorganic ion transport and metabolism
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 6694369 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9UHB4 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name Q9UHB4_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1794 bp
ATGCCGAGCCCGCAGCTTCTGGTGCTCTTCGGCAGCCAGACAGGCACGGCTCAGGATGTG
TCGGAGAGACTGGGTCGCGAGGCCCGGCGCCGGCGGCTTGGCTGCCGGGTGCAGGCCCTG
GACTCCTACCCGGTGGTGAATCTGATTAACGAGCCCCTGGTGATATTTGTTTGTGCAACT
ACAGGCCAAGGAGACCCCCCTGACAACATGAAGAACTTCTGGAGGTTTATATTCCGGAAG
AACCTGCCCTCCACTGCCCTCTGTCAGATGGACTTTGCCGTCCTGGGCCTCGGGGACTCC
TCATACGCCAAGTTCAACTTCGTGGCCAAGAAGCTGCACCGACGGCTACTGCAGCTTGGG
GGCAGCGCCCTCCTGCCCGTGTGCCTGGGCGATGACCAGCATGAGCTGGGGCCCGACGCT
GCTGTGGACCCCTGGCTGCGAGACTTGTGGGACAGGGTTCTGGGGCTGTACCCGCCGCCT
CCGGGCCTCACTGAGATCCCTCCCGGAGTCCCCCTGCCCTCCAAGTTCACCCTGCTGTTC
CTCCAAGAGGCACCCAGCACGGGCTCTGAGGGGCAGCGGGTAGCTCACCCCGGCTCTCAG
GAGCCCCCGTCAGAGTCGAAGCCCTTCCTAGCACCCATGATCTCCAACCAGAGAGTCACC
GGCCCCTCCCACTTCCAGGACGTTCGGCTGATTGAGTTTGACATCTTGGGCTCTGGCATC
AGCTTTGCTGCTGGTGATGTGGTGCTGATTCAGCCCTCCAACTCGGCTGCCCATGTCCAG
CGGTTCTGCCAGGTGCTGGGCCTGGACCCTGACCAGCTCTTCATGCTGCAGCCGCGGGAG
CCAGATGTCTCCTCCCCCACGAGGCTGCCCCAGCCCTGCTCCATGCGGCACCTCGTGTCC
CACTACCTGGACATCGCCAGCGTGCCTCGCCGCTCCTTCTTCGAACTCCTGGCCTGTCTA
TCCCTCCATGAGCTGGAGCGGGAGAAGCTGCTGGAGTTCAGTTCTGCCCAAGGCCAGGAG
GAGCTCTTTGAATACTGCAACCGGCCCCGCAGGACCATCCTGGAGGTGCTCTGTGACTTC
CCGCACACAGCTGCCGCCATCCCTCCCGACTACCTGTTGGACCTCATCCCCGTTATCCGG
CCGAGGGCCTTCTCCATCGCCTCCTCGCTGCTGACTCACCCCTCACGGCTGCAGATCCTC
GTGGCTGTAGTGCAGTTCCAGACTCGCCTCAAGGAGCCCCGCCGGGGCCTCTGCTCCTCC
TGGCTGGCATCCCTGGACCCTGGGCAAGGACCTGTCCGGGTGCCCCTCTGGGTGCGGCCT
GGGAGTCTGGCCTTCCCAGAGACACCAGACACACCTGTGATCATGGTGGGGCCTGGCACT
GGGGTAGCCCCCTTCCGAGCAGCCATCCAGGAGCGTGTGGCCCAGGGCCAGACTGGAAAC
TTCTTGTTTTTTGGCTGCCGCTGGCGGGACCAAGACTTCTACTGGGAGGCTGAGTGGCAG
GAGCTGGAGAAGCGGGACTGTCTGACCCTCATCCCTGCCTTCTCCCGGGAACAGGAGCAG
AAAGTATATGTGCAGCACCGGCTCCGGGAGCTGGGGTCGCTTGTGTGGGAACTGCTGGAC
CGCCAGGGTGCATACTTCTACCTGGCAGGCAACGCCAAGTCCATGCCAGCGGACGTCTCG
GAAGCCCTGATGTCCATCTTCCAGGAGGAGGGTGGACTCTGCAGCCCGGACGCAGCCGCG
TATCTAGCCAGGCTCCAGCAGACACGGCGCTTCCAGACAGAGACGTGGGCCTGA
Enzyme 22 GenBank Gene ID AF199509 Link Image
Enzyme 22 GeneCard ID Q9UHB4 Link Image
Enzyme 22 GenAtlas ID NDOR1 Link Image
Enzyme 22 HGNC ID HGNC:29838 Link Image
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Paine MJ, Garner AP, Powell D, Sibbald J, Sales M, Pratt N, Smith T, Tew DG, Wolf CR: Cloning and characterization of a novel human dual flavin reductase. J Biol Chem. 2000 Jan 14;275(2):1471-8. [PubMed Link Image]
  2. 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 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 14007
Enzyme 23 Name Iodotyrosine dehalogenase 1 precursor
Enzyme 23 Synonyms
  1. IYD-1
Enzyme 23 Gene Name IYD
Enzyme 23 Protein Sequence >Iodotyrosine dehalogenase 1 precursor
MYFLTPILVAILCILVVWIFKNADRSMEKKKGEPRTRAEARPWVDEDLKDSSDLHQAEED
ADEWQESEENVEHIPFSHNHYPEKEMVKRSQEFYELLNKRRSVRFISNEQVPMEVIDNVI
RTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNW
IKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTP
LNCGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQIMVTV
Enzyme 23 Number of Residues 289
Enzyme 23 Molecular Weight 33360
Enzyme 23 Theoretical pI 7.71
Enzyme 23 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 23 General Function Energy production and conversion
Enzyme 23 Specific Function Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-23
Enzyme 23 Transmembrane Regions
  • 215-235
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 31322698 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q6PHW0 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name IYD1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >870 bp
ATGTATTTCCTGACTCCCATCTTGGTAGCCATTCTCTGCATTTTGGTTGTGTGGATCTTT
AAAAATGCCGACAGAAGCATGGAGAAAAAGAAGGGGGAGCCTAGAACCAGGGCCGAAGCT
CGCCCCTGGGTGGATGAAGACTTAAAAGACAGCAGTGACCTGCACCAAGCAGAAGAAGAT
GCTGATGAATGGCAAGAATCAGAAGAAAATGTTGAACACATCCCCTTCTCTCATAACCAC
TATCCTGAGAAGGAAATGGTTAAGAGGTCTCAGGAATTTTATGAACTTCTCAATAAGAGA
CGGTCAGTCAGGTTCATAAGTAATGAGCAAGTCCCAATGGAAGTCATTGATAATGTCATC
AGAACGGCAGGAACAGCCCCGAGTGGGGCTCACACAGAGCCCTGGACCTTCGTGGTTGTG
AAGGACCCAGACGTGAAGCACAAGATTCGAAAGATCATTGAGGAGGAAGAGGAGATCAAC
TACATGAAAAGGATGGGACATCGCTGGGTCACAGACCTCAAGAAACTGAGAACCAACTGG
ATTAAAGAGTACTTGGATACTGCCCCTATTTTGATTCTCATTTTCAAACAAGTACATGGT
TTCGCCGCAAATGGCAAGAAAAAAGTCCACTACTACAATGAGATCAGTGTTTCCATCGCT
TGTGGCATCCTGCTAGCTGCCCTGCAGAATGCAGGTCTGGTGACTGTCACTACCACTCCT
CTCAACTGTGGCCCTCGACTGAGGGTGCTCCTGGGCCGCCCCGCACATGAAAAGCTGCTG
ATGCTGCTCCCCGTGGGGTACCCCAGCAAGGAGGCCACGGTGCCTGACCTCAAGCGCAAA
CCTCTGGACCAGATCATGGTGACAGTGTAG
Enzyme 23 GenBank Gene ID AY259176 Link Image
Enzyme 23 GeneCard ID Q6PHW0 Link Image
Enzyme 23 GenAtlas ID IYD Link Image
Enzyme 23 HGNC ID HGNC:21071 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 14008
Enzyme 24 Name tRNA wybutosine-synthesizing protein 1 homolog
Enzyme 24 Synonyms
  1. tRNA-yW-synthesizing protein
  2. Radical S-adenosyl methionine and flavodoxin domain- containing protein 1
Enzyme 24 Gene Name TYW1
Enzyme 24 Protein Sequence >tRNA wybutosine-synthesizing protein 1 homolog
MDPSADTWDLFSPLISLWINRFYIYLGFAVSISLWICVQIVIKTQGKNLQEKSVPKAAQD
LMTNGYVSLQEKDIFVSGVKIFYGSQTGTAKGFATVLAEAVTSLDLPVAIINLKEYDPDD
HLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRYAVFGLG
NSAYASHFNKVGKNVDKWLWMLGAHRVMSRGEGDCDVVKSKHGSIEADFRAWKTKFISQL
QALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSHEQDELHHRDTEEEEPFESSSEEEF
GGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPAL
REALTKQGYQLIGSHSGVKLCRWTKSMLRGRGGCYKHTFYGIESHRCMETTPSLACANKC
VFCWRHHTNPVGTEWRWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHC
ALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDS
LKKIDRPLFKDFWQRFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFI
EVKGVTYCGESSASSLTMAHVPWHEEVVQFVHELVDLIPEYEIACEHEHSNCLLIAHRKF
KIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGASERGFDPKDTRH
QRKNKSKAISGC
Enzyme 24 Number of Residues 732
Enzyme 24 Molecular Weight 83703
Enzyme 24 Theoretical pI 6.87
Enzyme 24 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Energy production and conversion
Enzyme 24 Specific Function Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 20-42
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 7023232 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q9NV66 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name TYW1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >2199 bp
ATGGATCCTTCTGCGGATACATGGGACCTCTTCTCACCTTTAATATCATTATGGATAAAC
AGGTTTTACATTTATTTGGGCTTTGCTGTTAGCATTAGCCTTTGGATTTGTGTCCAGATT
GTCATCAAGACGCAGGGCAAGAACTTACAGGAAAAATCTGTTCCAAAAGCAGCTCAGGAT
TTGATGACAAATGGTTATGTCTCCCTTCAAGAGAAAGACATCTTTGTGTCTGGAGTGAAG
ATTTTTTATGGTTCTCAGACTGGAACAGCAAAGGGATTCGCAACAGTTCTTGCTGAAGCA
GTTACATCCCTGGATCTGCCTGTGGCCATTATTAATCTAAAAGAATATGATCCAGATGAT
CATCTGATAGAAGAGGTGACTAGTAAAAATGTCTGTGTCTTCCTGGTTGCGACATACACT
GACGGCCTACCAACTGAAAGTGCAGAGTGGTTCTGCAAATGGTTAGAGGAAGCATCCATT
GATTTTCGATTTGGCAAAACTTACCTGAAGGGTATGAGATATGCGGTATTTGGCCTGGGA
AATTCTGCCTATGCTAGCCACTTCAACAAGGTTGGCAAAAATGTTGACAAGTGGCTCTGG
ATGCTTGGCGCGCATCGTGTGATGAGTCGAGGGGAGGGCGACTGCGACGTGGTTAAAAGC
AAGCACGGCAGCATTGAGGCCGACTTCAGAGCATGGAAGACCAAGTTCATCTCCCAGCTG
CAGGCACTTCAGAAAGGGGAGAGAAAGAAGTCCTGTGGCGGCCACTGCAAGAAAGGCAAA
TGTGAATCTCACCAACATGGCTCAGAGGAGAGGGAGGAAGGATCTCATGAGCAGGATGAA
TTGCATCATAGAGACACCGAGGAGGAAGAACCCTTTGAGAGCTCCAGTGAAGAAGAGTTT
GGTGGTGAGGACCATCAGAGCCTAAATTCCATTGTTGATGTTGAAGATTTGGGCAAAATT
ATGGATCATGTGAAGAAAGAAAAGAGAGAAAAGGAACAGCAGGAAGAGAAGTCTGGTTTG
TTCAGGAACATGGGGAGGAATGAAGATGGTGAAAGAAGAGCTATGATAACTCCTGCTCTC
CGAGAAGCCCTTACTAAACAAGGTTATCAGTTGATTGGGAGCCACTCGGGGGTGAAGCTT
TGCAGGTGGACAAAGTCCATGCTCCGAGGGAGAGGAGGTTGTTACAAACACACATTCTAT
GGAATTGAGAGCCATCGCTGCATGGAAACCACCCCGAGCTTGGCGTGTGCTAATAAATGT
GTCTTCTGTTGGCGGCACCACACCAACCCCGTGGGCACTGAGTGGCGGTGGAAGATGGAC
CAGCCTGAAATGATCTTGAAGGAAGCCATTGAAAACCATCAGAACATGATTAAGCAGTTT
AAAGGAGTACCGGGCGTCAAAGCAGAACGCTTTGAAGAAGGAATGACGGTAAAGCACTGT
GCATTGTCCCTCGTGGGAGAACCAATAATGTACCCAGAGATCAACAGGTTTTTGAAGCTA
CTCCACCAGTGTAAAATTTCCAGCTTCCTGGTCACAAACGCACAATTTCCTGCGGAAATC
AGGAACCTCGAGCCGGTTACTCAGCTGTATGTCAGTGTGGATGCCAGTACCAAAGACAGC
CTGAAGAAAATCGACCGCCCACTCTTCAAGGATTTCTGGCAGAGATTCCTTGACAGTTTA
AAAGCCTTGGCAGTCAAGCAACAACGAACTGTCTACAGACTGACGCTCGTGAAAGCATGG
AATGTGGACGAGCTCCAGGCCTACGCGCAGCTCGTGTCCCTGGGAAATCCTGACTTCATC
GAAGTGAAGGGCGTTACCTACTGCGGAGAAAGTTCAGCAAGCAGTCTTACCATGGCCCAC
GTGCCCTGGCATGAGGAAGTGGTACAGTTTGTCCGCGAGCTGGTGGATCTGATCCCCGAA
TATGAAATTGCATGTGAACACGAACACTCTAATTGCCTCCTGATAGCACACAGAAAGTTT
AAAATTGGTGGTGAATGGTGGACATGGATCAATTATAACCGCTTCCAGGAGCTCATCCAG
GAATATGAAGATAGTGGTGGATCAAAAACGTTCAGCGCAAAGGATTATATGGCCAGAACT
CCTCACTGGGCATTATTTGGTGCCAGTGAAAGAGGCTTTGATCCCAAGGACACAAGACAT
CAGAGAAAGAACAAATCAAAGGCTATTTCTGGATGTTGA
Enzyme 24 GenBank Gene ID AK001762 Link Image
Enzyme 24 GeneCard ID Q9NV66 Link Image
Enzyme 24 GenAtlas ID TYW1 Link Image
Enzyme 24 HGNC ID HGNC:25598 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 14009
Enzyme 25 Name tRNA wybutosine-synthesizing protein 1 homolog B
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name Not Available
Enzyme 25 Protein Sequence >tRNA wybutosine-synthesizing protein 1 homolog B
MDPSADTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIEMQGFATVLAEAVTSLDL
PVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGK
TYLKGMRDAVFGLGNSAYASHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVVKSKHGSIE
ANFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSQEQDELHHRDT
KEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGR
NEDGERRAMITPALREALTKQVDAPRERSLLQTHILWNESHRCMETTPSLACANKCVFCW
WHHNNPVGTEWLWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSL
VGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKI
DRPLFKDFWQQFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFIEVKG
VTYCRESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAHRKFKIGG
EWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGANERSFDPKDTRHQRKN
KSKAISGC
Enzyme 25 Number of Residues 668
Enzyme 25 Molecular Weight 76917
Enzyme 25 Theoretical pI 6.22
Enzyme 25 GO Classification
Function
  • FMN binding
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • nucleotide binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 25 General Function Energy production and conversion
Enzyme 25 Specific Function Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 20-42
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 46250014 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q6NUM6 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name TYW1B_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2007 bp
ATGGATCCTTCTGCGGATACATGGGACCTCTCCTCACCTTTAATATCATTATGGATAAAC
AGGTTTTACATTTATCTGGGCTTTGCTGTTAGCATTAGCCTTTGGATTTGTGTCCAGATT
GTCATCGAGATGCAGGGATTTGCAACAGTTCTTGCTGAAGCAGTTACGTCCCTGGATCTG
CCTGTGGCCATTATTAATCTAAAAGAATATGATCCAGATGATCATCTGATAGAAGAGGTG
ACTAGTAAAAATGTCTGTGTCTTCCTGGTTGCGACATACACTGACGGCCTACCAACCGAA
AGTGCAGAGTGGTTCTGCAAATGGTTAGAGGAAGCATCCATTGATTTTCGATTTGGCAAA
ACTTACCTGAAGGGTATGAGAGATGCGGTATTTGGCCTGGGAAATTCTGCCTATGCTAGC
CACTTCAACAAGGTTGGCAAAAATGTTGACAAGTGGCTCTGGATGCTTGGCGTGCATCGT
GTGATGAGTCGAGGGGAGGGCGACTGCGACGTGGTTAAAAGCAAGCACGGCAGCATTGAG
GCCAACTTCAGAGCATGGAAGACCAAGTTCATCTCCCAGCTGCAGGCACTTCAGAAAGGG
GAGAGAAAGAAGTCCTGTGGCGGCCACTGCAAGAAAGGCAAATGTGAATCTCACCAACAT
GGCTCAGAGGAGAGGGAGGAAGGATCTCAAGAGCAGGACGAATTGCATCACAGAGACACC
AAGGAGGAAGAACCCTTCGAGAGCTCCAGTGAAGAAGAGTTTGGTGGTGAGGACCATCAG
AGCCTAAATTCCATTGTTGATGTTGAAGATTTGGGCAAAATTATGGATCACGTGAAGAAA
GAAAAGAGAGAAAAGGAACAGCAGGAAGAGAAGTCTGGTTTGTTCAGGAACATGGGGAGG
AATGAAGATGGTGAAAGAAGAGCTATGATAACTCCTGCTCTCCGAGAAGCCCTTACTAAA
CAAGTCGATGCTCCGAGGGAGAGGAGCTTGTTACAAACACACATTCTATGGAATGAGAGC
CATCGCTGCATGGAAACCACCCCGAGCTTGGCGTGTGCTAATAAATGTGTCTTCTGTTGG
TGGCACCACAACAACCCTGTGGGCACTGAATGGTTGTGGAAGATGGACCAGCCTGAAATG
ATCTTGAAGGAAGCCATTGAAAACCATCAGAACATGATTAAGCAGTTTAAAGGAGTACCG
GGCGTCAAAGCAGAACGCTTTGAAGAAGGAATGACGGTAAAGCACTGTGCATTGTCCCTC
GTGGGAGAACCAATAATGTACCCAGAGATCAACAGGTTTTTGAAGCTACTCCACCAGTGT
AAAATCTCCAGCTTCCTGGTCACAAATGCACAATTTCCTGCGGAAATCAGGAACCTCGAG
CCAGTTACTCAGCTGTATGTCAGTGTGGATGCCAGTACCAAAGACAGCCTGAAGAAAATC
GACCGCCCACTCTTCAAGGATTTCTGGCAGCAATTCCTTGACAGTTTAAAAGCCTTGGCA
GTCAAGCAACAACGAACTGTCTACAGACTGACGCTCGTGAAAGCATGGAACGTGGACGAG
CTCCAGGCCTACGCGCAGCTCGTGTCCCTGGGGAATCCTGACTTCATCGAAGTGAAGGGC
GTTACCTACTGCAGAGAAAGTTCAGCAAGCAGTCTTACCATGGCCCATGTGCCCTGGCAT
GAGGAAGTGGTACAGTTTGTCCGCGAGCTGGTGGATCTGATCCCCGAATATGAAATTGCA
TGTGAACACGAACACTCTAATTGCCTCCTGATAGCACACAGAAAGTTTAAAATTGGTGGT
GAATGGTGGACATGGATCGATTATAACCGCTTCCAGGAGCTCATCCAGGAATATGAAGAT
AGTGGTGGATCAAAAACGTTCAGCGCAAAGGATTATATGGCCAGAACTCCTCACTGGGCA
TTATTTGGTGCCAATGAAAGAAGCTTTGATCCCAAGGACACAAGACATCAGAGAAAGAAC
AAATCAAAGGCTATTTCTGGATGTTGA
Enzyme 25 GenBank Gene ID BC068520 Link Image
Enzyme 25 GeneCard ID Q6NUM6 Link Image
Enzyme 25 GenAtlas ID TYW1B Link Image
Enzyme 25 HGNC ID HGNC:33908 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs Not Available
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15208
Enzyme 26 Name cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a)
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name HAO1
Enzyme 26 Protein Sequence >cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a)
MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET
DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE
AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ
LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR
GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV
LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV
RKNPLAVSKI
Enzyme 26 Number of Residues 370
Enzyme 26 Molecular Weight 40925
Enzyme 26 Theoretical pI 8.29
Enzyme 26 GO Classification Not Available
Enzyme 26 General Function Energy production and conversion
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function Not Available
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 158259869 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A8K058 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A8K058_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1113 bp
ATGCTCCCCCGGCTAATTTGTATCAATGATTATGAACAACATGCTAAATCAGTACTTCCA
AAGTCTATATATGACTATTACAGGTCTGGGGCAAATGATGAAGAAACTTTGGCTGATAAT
ATTGCAGCATTTTCCAGATGGAAGCTGTATCCAAGGATGCTCCGGAATGTTGCTGAAACA
GATCTGTCGACTTCTGTTTTAGGACAGAGGGTCAGCATGCCAATATGTGTGGGGGCTACG
GCCATGCAGCGCATGGCTCATGTGGACGGCGAGCTTGCCACTGTGAGAGCCTGTCAGTCC
CTGGGAACGGGCATGATGTTGAGTTCCTGGGCCACCTCCTCAATTGAAGAAGTGGCGGAA
GCTGGTCCTGAGGCACTTCGTTGGCTGCAACTGTATATCTACAAGGACCGAGAAGTCACC
AAGAAGCTAGTGCGGCAGGCAGAGAAGATGGGCTACAAGGCCATATTTGTGACAGTGGAC
ACACCTTACCTGGGCAACCGTCTGGATGATGTGCGTAACAGATTCAAACTGCCGCCACAA
CTCAGGATGAAAAATTTTGAAACCAGTACTTTATCATTTTCTCCTGAGGAAAATTTTGGA
GACGACAGTGGACTTGCTGCATATGTGGCTAAAGCAATAGACCCATCTATCAGCTGGGAA
GATATCAAATGGCTGAGAAGACTGACATCATTGCCAATTGTTGCAAAGGGCATTTTGAGA
GGTGATGATGCCAGGGAGGCTGTTAAACATGGCTTGAATGGGATCTTGGTGTCGAATCAT
GGGGCTCGACAACTCGATGGGGTGCCAGCCACTATTGATGTTCTGCCAGAAATTGTGGAG
GCTGTGGAAGGGAAGGTGGAAGTCTTCCTGGACGGGGGTGTGCGGAAAGGCACTGATGTT
CTGAAAGCTCTGGCTCTTGGCGCCAAGGCTGTGTTTGTGGGGAGACCAATCGTTTGGGGC
TTAGCTTTCCAGGGGGAGAAAGGTGTTCAAGATGTCCTCGAGATACTAAAGGAAGAATTC
CGGTTGGCCATGGCTCTGAGTGGGTGCCAGAATGTGAAAGTCATCGACAAGACATTGGTG
AGGAAAAATCCTTTGGCCGTTTCCAAGATCTGA
Enzyme 26 GenBank Gene ID AK289423 Link Image
Enzyme 26 GeneCard ID A8K058 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location 20
Enzyme 26 Locus 20p12
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 15247
Enzyme 27 Name Testicular acid phosphatase
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name ACPT
Enzyme 27 Protein Sequence >Testicular acid phosphatase
MAGLGFWGHPAGPLLLLLLLVLPPRALPEGPLVFVALVFRHGDRAPLASYPMDPHKEVAS
TLWPRGLGQLTTEGVRQQLELGRFLRSRYEAFLSPEYRREEVYIRSTDFDRTLESAQANL
AGLFPEAAPGSPEARWRPIPVHTVPVAEDKLLRFPMRSCPRYHELLREATEAAEYQEALE
GWTGFLSRLENFTGLSLVGEPLRRAWKVLDTLMCQQAHGLPLPAWASPDVLRTLAQISAL
DIGAHVGPPRAAEKAQLTGGILLNAILANFSRVQRLGLPLKMVMYSAHDSTLLALQGALG
LYDGHTPPYAACLGFEFRKHLGNPAKDGGNVTVSLFYRNDSAHLPLPLSLPGCPAPCPLG
RFYQLTAPARPPAHGVSCHGPYEAAIPPAPVVPLLAGAVAVLVALSLGLGLLAWRPGCLR
ALGGPV
Enzyme 27 Number of Residues 426
Enzyme 27 Molecular Weight 46090
Enzyme 27 Theoretical pI 8.29
Enzyme 27 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
Component
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Dephosphorylates receptor tyrosine-protein kinase erbB-4 and inhibits the ligand-induced proteolytic cleavage
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-26
Enzyme 27 Transmembrane Regions
  • 394-414
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 12958660 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q9BZG2 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PPAT_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1281 bp
ATGGCCGGCCTGGGGTTTTGGGGCCACCCTGCTGGACCTCTCCTGCTGCTGCTGCTGCTG
GTGCTGCCACCCCGGGCCCTGCCAGAAGGACCCCTGGTGTTCGTGGCTCTGGTATTCCGC
CATGGCGACCGGGCCCCGCTGGCCTCCTACCCCATGGACCCACACAAGGAGGTGGCCTCC
ACCCTGTGGCCACGAGGCCTGGGCCAGCTGACCACGGAGGGGGTCCGCCAGCAGCTGGAG
CTGGGCCGCTTCCTGAGGAGCCGCTACGAGGCCTTCCTGAGTCCGGAGTACCGGCGGGAG
GAGGTGTACATCCGCAGCACGGACTTTGACCGCACGCTGGAGAGTGCCCAGGCCAACCTT
GCCGGGCTGTTTCCCGAGGCTGCTCCAGGGAGCCCCGAGGCCCGCTGGAGGCCGATCCCG
GTGCACACGGTGCCCGTGGCTGAGGATAAGCTGCTGAGGTTCCCCATGCGCAGCTGTCCC
CGATACCACGAGCTGCTGCGGGAGGCCACCGAGGCCGCCGAGTACCAGGAGGCCCTGGAG
GGCTGGACGGGCTTCCTGAGTCGCCTGGAGAACTTCACGGGACTGTCGCTGGTTGGAGAG
CCACTGCGCAGGGCATGGAAGGTTCTGGACACCCTCATGTGCCAGCAAGCCCACGGTCTT
CCACTACCAGCCTGGGCCTCCCCAGATGTCCTGCGGACTCTTGCCCAGATCTCGGCTTTG
GATATTGGAGCCCACGTGGGCCCACCCCGGGCAGCAGAGAAGGCCCAGCTGACAGGGGGG
ATCCTGCTGAATGCTATCCTTGCAAACTTCTCCCGGGTCCAGCGCCTGGGGCTGCCCCTC
AAGATGGTCATGTACTCAGCTCATGACAGCACCCTGCTGGCCCTCCAGGGGGCCCTGGGC
CTCTATGATGGACACACCCCGCCATATGCTGCCTGCCTCGGCTTTGAGTTCCGGAAGCAC
CTGGGGAATCCCGCCAAAGATGGAGGGAATGTCACCGTCTCCCTCTTCTACCGCAATGAC
TCCGCCCACCTGCCCCTGCCTCTCAGCCTCCCCGGGTGCCCGGCCCCCTGTCCACTAGGC
CGCTTCTACCAGCTGACTGCCCCGGCCCGGCCTCCCGCCCATGGGGTCTCCTGCCATGGC
CCCTATGAGGCTGCCATCCCCCCAGCTCCAGTGGTGCCCCTGCTGGCCGGAGCTGTAGCT
GTGCTGGTGGCACTCAGCTTGGGGCTGGGCCTGCTGGCCTGGAGACCAGGGTGCCTGCGG
GCCTTGGGGGGCCCCGTGTGA
Enzyme 27 GenBank Gene ID AF321918 Link Image
Enzyme 27 GeneCard ID Q9BZG2 Link Image
Enzyme 27 GenAtlas ID ACPT Link Image
Enzyme 27 HGNC ID HGNC:14376 Link Image
Enzyme 27 Chromosome Location 19
Enzyme 27 Locus 19q13.4
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Yousef GM, Diamandis M, Jung K, Diamandis EP: Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis. Genomics. 2001 Jun 15;74(3):385-95. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16490
Enzyme 28 Name Sarcosine dehydrogenase
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name SARDH
Enzyme 28 Protein Sequence >Sarcosine dehydrogenase
MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPS
RPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSD
VEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESH
VLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGI
RVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTER
IEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQH
IEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGC
GQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAG
RNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRR
LLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSR
PPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHI
TTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGH
LVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHW
HADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLE
AIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQ
AHLKSPFDPNNKRVKGIY
Enzyme 28 Number of Residues 918
Enzyme 28 Molecular Weight 101038
Enzyme 28 Theoretical pI 7.26
Enzyme 28 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • oxidoreductase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • glycine catabolism
  • glycine metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 28 General Function Amino acid transport and metabolism
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID B2RMR5 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B2RMR5_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID BC136363 Link Image
Enzyme 28 GeneCard ID B2RMR5 Link Image
Enzyme 28 GenAtlas ID SARDH Link Image
Enzyme 28 HGNC ID HGNC:10536 Link Image
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16534
Enzyme 29 Name Putative uncharacterized protein ACP1
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name ACP1
Enzyme 29 Protein Sequence >Putative uncharacterized protein ACP1
MAEQATKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRG
QSCMKRHGIPMSHVARQVPSLDLKLCVLCFSGSLTAVLFLTGTWAGPQTQEL
Enzyme 29 Number of Residues 112
Enzyme 29 Molecular Weight 12230
Enzyme 29 Theoretical pI 7.85
Enzyme 29 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoprotein phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
  • protein tyrosine phosphatase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid dephosphorylation
  • protein modification
Component
Enzyme 29 General Function Signal transduction mechanisms
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein Not Available
Enzyme 29 UniProtKB/Swiss-Prot ID B5MCC7 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name B5MCC7_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AC079779 Link Image
Enzyme 29 GeneCard ID B5MCC7 Link Image
Enzyme 29 GenAtlas ID ACP1 Link Image
Enzyme 29 HGNC ID HGNC:122 Link Image
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available