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Human Metabolome Database Version 2.5

 

Showing metabocard for 3-Hydroxyanthranilic acid (HMDB01476)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-16 16:50:01
Accession Number HMDB01476
Secondary Accession Numbers Not Available
Common Name 3-Hydroxyanthranilic acid
Description An oxidation product of tryptophan metabolism. It may be a free radical scavenger and a carcinogen.
Synonyms
  1. 2-Amino-3-hydroxybenzoate
  2. 2-Amino-3-hydroxybenzoic acid
  3. 2-amino-3-hydroxy-Benzoate
  4. 2-amino-3-hydroxy-Benzoic acid
  5. 3-Hydroxy-2-aminobenzoate
  6. 3-Hydroxy-2-aminobenzoic acid
  7. 3-Hydroxy-anthranilsaeure
  8. 3-hydroxyanthranilic acid
  9. 3-Hydroxyanthranilate
  10. 3-OHAA
  11. 3-OH-anthranilic acid
  12. 3-Oxyanthranilate
  13. 3-Oxyanthranilic acid
  14. 3-hydroxanthranilate
  15. 3-hydroxyantranilic acid
  16. 3-hydroxy-Anthranilate
  17. 3-hydroxy-Anthranilic acid
Chemical IUPAC Name 2-amino-3-hydroxy-benzoic acid
Chemical Formula C7H7NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • aromatic compound
Biofunction
  • Component of Tryptophan metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 153.135
Monoisotopic Molecular Weight 153.042587
Isomeric SMILES NC1=C(O)C=CC=C1C(O)=O
Canonical SMILES NC1=C(O)C=CC=C1C(O)=O
KEGG Compound ID C00632 Link Image
BioCyc ID 3-HYDROXY-ANTHRANILATE Link Image
BiGG ID 1485273 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01476 Link Image
Metagene Link HMDB01476 Link Image
METLIN ID 3275 Link Image
PubChem Compound 86 Link Image
PubChem Substance 7885274 Link Image
ChEBI ID 15793 Link Image
CAS Registry Number 548-93-6
InChI Identifier InChI=1/C7H7NO3/c8-6-4(7(10)11)2-1-3-5(6)9/h1-3,9H,8H2,(H,10,11)
Synthesis Reference Warnell, J. L. 3-Hydroxyanthranilic acid. Biochemical Preparations (1958), 6 20-4.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 10.5 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.81 [Predicted by ALOGPS]; 1.012 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
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
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
  • Cytoplasm
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Bladder —
Epidermis —
Lymphocyte —
Concentrations (Normal)
Biofluid Blood
Value 0.079 (0.015-0.209) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Herve C, Beyne P, Jamault H, Delacoux E: Determination of tryptophan and its kynurenine pathway metabolites in human serum by high-performance liquid chromatography with simultaneous ultraviolet and fluorimetric detection. J Chromatogr B Biomed Appl. 1996 Jan 12;675(1):157-61. [PubMed Link Image]
Biofluid Urine
Value 3.28 (0.46-5.19) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Concentrations (Abnormal)
Biofluid Blood
Value 0.01 (0.007-0.011) uM
Age Adult:>18 yrs old
Sex Both
Condition Stroke
Comments Not Available
References
  • Darlington LG, Mackay GM, Forrest CM, Stoy N, George C, Stone TW: Altered kynurenine metabolism correlates with infarct volume in stroke. Eur J Neurosci. 2007 Oct;26(8):2211-21. Epub 2007 Sep 24. [PubMed Link Image]
Associated Disorders
Condition References
Stroke
  • Darlington LG, Mackay GM, Forrest CM, Stoy N, George C, Stone TW: Altered kynurenine metabolism correlates with infarct volume in stroke. Eur J Neurosci. 2007 Oct;26(8):2211-21. Epub 2007 Sep 24. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References
  1. Calandra P: Research on tryptophan metabolites "via kynurenine" in epidermis of man and mouse. Acta Vitaminol Enzymol. 1975;29(1-6):158-60. [PubMed Link Image]
  2. Werner ER, Lutz H, Fuchs D, Hausen A, Huber C, Niederwieser D, Pfleiderer W, Reibnegger G, Troppmair J, Wachter H: Identification of 3-hydroxyanthranilic acid in mixed lymphocyte cultures. Biol Chem Hoppe Seyler. 1985 Jan;366(1):99-102. [PubMed Link Image]
  3. Teulings FA, Mulder-Kooy GE, Peters HA, Fokkens W, Van Der Werf-Messing B: The excretion of 3-hydroxyanthranilic acid in patients with bladder and kidney carcinoma. Acta Vitaminol Enzymol. 1975;29(1-6):108-12. [PubMed Link Image]
  4. De Antoni A, Rubaltelli FF, Costa C, Allegri G: Effect of phototherapy on the urinary excretion of tryptophan metabolites in neonatal hyperbilirubinemia. Acta Vitaminol Enzymol. 1975;29(1-6):145-50. [PubMed Link Image]
  5. Lopez AS, Alegre E, LeMaoult J, Carosella E, Gonzalez A: Regulatory role of tryptophan degradation pathway in HLA-G expression by human monocyte-derived dendritic cells. Mol Immunol. 2006 Jul;43(14):2151-60. Epub 2006 Feb 21. [PubMed Link Image]
  6. Yeh JK, Brown RR: Effects of vitamin B-6 deficiency and tryptophan loading on urinary excretion of tryptophan metabolites in mammals. J Nutr. 1977 Feb;107(2):261-71. [PubMed Link Image]
  7. Herve C, Beyne P, Jamault H, Delacoux E: Determination of tryptophan and its kynurenine pathway metabolites in human serum by high-performance liquid chromatography with simultaneous ultraviolet and fluorimetric detection. J Chromatogr B Biomed Appl. 1996 Jan 12;675(1):157-61. [PubMed Link Image]
  8. Hegedus ZL, Frank HA, Altschule MD, Nayak U: Human plasma lipofuscin melanins formed from tryptophan metabolites. Arch Int Physiol Biochim. 1986 Dec;94(5):339-48. [PubMed Link Image]
  9. Teulings FA, Lems PH, Portengen H, Henkelman MS, Blonk DI: The action of 3-hydroxyanthranilic acid and other tryptophan metabolites on stimulated human lymphocytes. Acta Vitaminol Enzymol. 1975;29(1-6):113-6. [PubMed Link Image]
Metabolic Enzymes
  1. 3-hydroxyanthranilate 3,4-dioxygenase
  2. Catalase
  3. Kynureninase
  4. cDNA FLJ78138, highly similar to Homo sapiens catalase
Enzyme 1 [top]
Enzyme 1 ID 6424
Enzyme 1 Name 3-hydroxyanthranilate 3,4-dioxygenase
Enzyme 1 Synonyms
  1. 3-HAO
  2. 3- hydroxyanthranilic acid dioxygenase
  3. 3-hydroxyanthranilate oxygenase
Enzyme 1 Gene Name HAAO
Enzyme 1 Protein Sequence >3-hydroxyanthranilate 3,4-dioxygenase 
MERRLGVRAWVKENRGSFQPPVCNKLMHQEQLKVMFVGGPNTRKDYHIEEGEEVFYQLEG
DMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYV
GDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKPIPDQLLKEPPFPLSTRSIMEP
MSLDAWLDSHHRELQAGTPLSLFGDTYETQVIAYGQGSSEGLRQNVDVWLWQLEGSSVVT
MGGRRLSLAPDDSLLVLAGTSYAWERTQGSVALSVTQDPACKKPLG
Enzyme 1 Number of Residues 286
Enzyme 1 Molecular Weight 32543
Enzyme 1 Theoretical pI 5.69
Enzyme 1 GO Classification
Function
  • 3-hydroxyanthranilate 3,4-dioxygenase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the synthesis of the excitotoxin quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. The direct product of the reaction spontaneously rearrange to QUIN
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 443919 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P46952 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name 3HAO_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >861 bp 
ATGGAGCGCCGCCTGGGAGTGAGGGCCTGGGTGAAGGAGAACCGGGGCTCCTTCCAGCCC
CCGGTCTGCAACAAGCTCATGCACCAGGAGCAGCTCAAAGTCATGTTCGTCGGAGGCCCC
AACACCAGGAAGGACTATCACATCGAAGAGGGTGAAGAGGTATTTTACCAGCTGGAGGGA
GACATGGTTCTCCGAGTCCTGGAGCAAGGGAAACACCGGGATGTGGTCATTCGGCAGGGA
GAGATATTCCTCCTGCCTGCCAGGGTGCCCCACTCACCACAGAGGTTTGCCAACACCGTG
GGGCTGGTGGTTGAGCGAAGGCGGCTGGAGACCGAGCTAGATGGGCTCAGGTACTATGTG
GGCGACACCATGGACGTTCTGTTTGAGAAGTGGTTCTACTGCAAGGACCTCGGCACGCAG
TTGGCCCCCATCATCCAGGAGTTCTTCAGCTCTGAGCAGTACAGAACAGGAAAGCCCATC
CCTGACCAGCTGCTCAAGGAGCCACCATTCCCTCTGAGCACACGATCCATCATGGAGCCC
ATGTCCCTGGATGCCTGGCTGGACAGCCACCACAGGGAGCTGCAGGCAGGCACACCACTC
AGCCTGTTTGGGGACACCTATGAGACCCAGGTGATCGCCTATGGGCAAGGCAGCAGCGAA
GGCCTGAGACAGAATGTGGACGTGTGGCTGTGGCAGCTGGAGGGCTCCTCGGTGGTGACA
ATGGGGGGACGGCGCCTGAGCCTGGCCCCTGATGACAGCCTCCTGGTGCTAGCTGGGACC
TCGTATGCCTGGGAGCGAACACAAGGCTCTGTGGCCCTGTCTGTGACCCAGGACCCTGCC
TGCAAGAAGCCCCTGGGGTGA
Enzyme 1 GenBank Gene ID Z29481 Link Image
Enzyme 1 GeneCard ID HAAO Link Image
Enzyme 1 GenAtlas ID HAAO Link Image
Enzyme 1 HGNC ID HGNC:4796 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Malherbe P, Kohler C, Da Prada M, Lang G, Kiefer V, Schwarcz R, Lahm HW, Cesura AM: Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase. J Biol Chem. 1994 May 13;269(19):13792-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6878
Enzyme 2 Name Catalase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name CAT
Enzyme 2 Protein Sequence >Catalase 
MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDE
MAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGES
GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPD
MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ
GIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLT
KVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPD
THRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALE
HSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVK
NFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
Enzyme 2 Number of Residues 527
Enzyme 2 Molecular Weight 59757
Enzyme 2 Theoretical pI 7.41
Enzyme 2 GO Classification
Function
  • antioxidant activity
  • catalase activity
  • peroxidase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
—
Enzyme 2 General Function Inorganic ion transport and metabolism
Enzyme 2 Specific Function Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 2 H2O2 = O2 + 2 H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1228085 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P04040 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CATA_HUMAN Link Image
Enzyme 2 PDB ID 1F4J Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >66 bp 
ATGGCTGACAGCCGGGATCCCGCCAGCGACCAGATGCAGCACTGGAAGGAGCAGCGGGCC
GCGCAG
Enzyme 2 GenBank Gene ID X04085 Link Image
Enzyme 2 GeneCard ID CAT Link Image
Enzyme 2 GenAtlas ID CAT Link Image
Enzyme 2 HGNC ID HGNC:1516 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Quan F, Korneluk RG, Tropak MB, Gravel RA: Isolation and characterization of the human catalase gene. Nucleic Acids Res. 1986 Jul 11;14(13):5321-35. [PubMed Link Image]
  2. Bell GI, Najarian RC, Mullenbach GT, Hallewell RA: cDNA sequence coding for human kidney catalase. Nucleic Acids Res. 1986 Jul 11;14(13):5561-2. [PubMed Link Image]
  3. Jin LH, Bahn JH, Eum WS, Kwon HY, Jang SH, Han KH, Kang TC, Won MH, Kang JH, Cho SW, Park J, Choi SY: Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells. Free Radic Biol Med. 2001 Dec 1;31(11):1509-19. [PubMed Link Image]
  4. Yoo JH, Erzurum SC, Hay JG, Lemarchand P, Crystal RG: Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress. J Clin Invest. 1994 Jan;93(1):297-302. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Korneluk RG, Quan F, Lewis WH, Guise KS, Willard HF, Holmes MT, Gravel RA: Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. J Biol Chem. 1984 Nov 25;259(22):13819-23. [PubMed Link Image]
  7. Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ: Structure of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. [PubMed Link Image]
  8. Putnam CD, Arvai AS, Bourne Y, Tainer JA: Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol. 2000 Feb 11;296(1):295-309. [PubMed Link Image]
  9. Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP: Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13118
Enzyme 3 Name Kynureninase
Enzyme 3 Synonyms
  1. L-kynurenine hydrolase
  2. Kynureninase
  3. L-kynurenine hydrolase, isoform CRA_a
Enzyme 3 Gene Name KYNU
Enzyme 3 Protein Sequence >Kynureninase 
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
Enzyme 3 Number of Residues 307
Enzyme 3 Molecular Weight 34635
Enzyme 3 Theoretical pI 5.71
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
  • kynureninase activity
  • pyridoxal phosphate binding
  • vitamin binding
Process
  • NAD biosynthesis
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • indolalkylamine metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
  • tryptophan catabolism
  • tryptophan metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 12654129 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9BVW3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q9BVW3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID BC000879 Link Image
Enzyme 3 GeneCard ID Q9BVW3 Link Image
Enzyme 3 GenAtlas ID KYNU Link Image
Enzyme 3 HGNC ID HGNC:6469 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13119
Enzyme 4 Name cDNA FLJ78138, highly similar to Homo sapiens catalase
Enzyme 4 Synonyms
  1. CAT, mRNA
  2. Catalase, isoform CRA_a
Enzyme 4 Gene Name CAT
Enzyme 4 Protein Sequence >cDNA FLJ78138, highly similar to Homo sapiens catalase 
MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDE
MAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGES
GSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPD
MVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQ
GIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLT
KVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPD
THRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALE
HSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVK
NFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
Enzyme 4 Number of Residues 527
Enzyme 4 Molecular Weight 59757
Enzyme 4 Theoretical pI 7.41
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Inorganic ion transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 158256602 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8K6C0 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K6C0_HUMAN Link Image
Enzyme 4 PDB ID 1F4J Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK291585 Link Image
Enzyme 4 GeneCard ID A8K6C0 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available