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Human Metabolome Database Version 2.5

 

Showing metabocard for Formylanthranilic acid (HMDB04089)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 11:37:45
Update Date 2010-03-16 15:50:37
Accession Number HMDB04089
Secondary Accession Numbers Not Available
Common Name Formylanthranilic acid
Description Formylanthranilic acid is a polar acid metabolite of anthranilic acid, occasionally found in human urine. (PMID 7320161)
Synonyms
  1. 2-(Formylamino)-benzoic acid
  2. 2-(formylamino)benzoate
  3. 2-formamidobenzoate
  4. Formylanthranilate
  5. N-Formylanthranilate
  6. 2-(Formylamino)-benzoate
  7. 2-(formylamino)benzoic acid
  8. 2-formamidobenzoic acid
Chemical IUPAC Name 2-formamidobenzoate
Chemical Formula C8H7NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Aminobenzoates
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • secondary carboxylic acid amide
  • aromatic compound
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 165.146
Monoisotopic Molecular Weight 165.042587
Isomeric SMILES OC(=O)C1=CC=CC=C1NC=O
Canonical SMILES OC(=O)C1=CC=CC=C1NC=O
KEGG Compound ID C05653 Link Image
BioCyc ID Not Available
BiGG ID 46205 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB04089 Link Image
Metagene Link HMDB04089 Link Image
METLIN ID Not Available
PubChem Compound 5459905 Link Image
PubChem Substance 8143772 Link Image
ChEBI ID 18410 Link Image
CAS Registry Number 3342-77-6
InChI Identifier InChI=1/C8H7NO3/c10-5-9-7-4-2-1-3-6(7)8(11)12/h1-5H,(H,9,10)(H,11,12)
Synthesis Reference Prashad, Mahavir; Har, Denis; Repic, Oljan; Blacklock, Thomas J.; Chin, Jefferson A.; Shapiro, Michael J. Reaction of benzoyleneurea and isatoic anhydride with the Vilsmeier reagent. Tetrahedron Letters (1997), 38(8), 1313-1316.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.33 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.28 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
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Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References Not Available
Metabolic Enzymes
  1. Probable arylformamidase
  2. Kynureninase
  3. AFMID protein
Enzyme 1 [top]
Enzyme 1 ID 13059
Enzyme 1 Name Probable arylformamidase
Enzyme 1 Synonyms
  1. Kynurenine formamidase
  2. KF
Enzyme 1 Gene Name AFMID
Enzyme 1 Protein Sequence >Probable arylformamidase 
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNNPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQVLPVQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQ
IILKTIFQ
Enzyme 1 Number of Residues 308
Enzyme 1 Molecular Weight 34556
Enzyme 1 Theoretical pI 5.78
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites
Enzyme 1 Pathways
Enzyme 1 Reactions
  • N-formyl-L-kynurenine + H2O = formate + L-kynurenine [RN:R01959] ALL_REAC R01959
  • (other) R00988 R04911
Enzyme 1 Pfam Domain Function Not Available
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 52545961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q63HM1 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AFMID_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence Not Available
Enzyme 1 GenBank Gene ID BX648442 Link Image
Enzyme 1 GeneCard ID Q63HM1 Link Image
Enzyme 1 GenAtlas ID AFMID Link Image
Enzyme 1 HGNC ID HGNC:20910 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References Not Available
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13118
Enzyme 2 Name Kynureninase
Enzyme 2 Synonyms
  1. L-kynurenine hydrolase
  2. Kynureninase
  3. L-kynurenine hydrolase, isoform CRA_a
Enzyme 2 Gene Name KYNU
Enzyme 2 Protein Sequence >Kynureninase 
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
Enzyme 2 Number of Residues 307
Enzyme 2 Molecular Weight 34635
Enzyme 2 Theoretical pI 5.71
Enzyme 2 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 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12654129 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BVW3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q9BVW3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID BC000879 Link Image
Enzyme 2 GeneCard ID Q9BVW3 Link Image
Enzyme 2 GenAtlas ID KYNU Link Image
Enzyme 2 HGNC ID HGNC:6469 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15219
Enzyme 3 Name AFMID protein
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name AFMID
Enzyme 3 Protein Sequence >AFMID protein 
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNSPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQIILKT
IFQ
Enzyme 3 Number of Residues 303
Enzyme 3 Molecular Weight 33992
Enzyme 3 Theoretical pI 5.78
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Lipid 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 124375910 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A2RUB3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A2RUB3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >912 bp 
ATGATGGATGTGTCTGGTGTGGGTTTCCCAAGCAAGGTTCCTTGGAAGAAGATGTCTGCA
GAGGAGCTGGAGAATCAGTACTGTCCCAGCCGATGGGTTGTCCGACTGGGAGCAGAGGAA
GCCTTGAGGACCTACTCACAGATAGGAATTGAAGCCACCACAAGGGCCCGGGCCACCAGG
AAGAGCCTGCTGCATGTCCCCTATGGAGACGGCGAAGGGGAGAAAGTGGACATTTACTTC
CCCGACGAGTCGTCTGAAGCCTTGCCTTTCTTCCTGTTCTTTCACGGAGGATACTGGCAG
AGCGGAAGTAAGGATGAGTCTGCCTTCATGGTCCACCCGCTGACGGCACAGGGAGTGGCC
GTGGTAATAGTGGCTTACGGCATCGCCCCCAAAGGCACCCTGGACCACATGGTAGACCAG
GTGACCCGCAGCGTTGCGTTTGTCCAGAAGCGGTATCCAAGCAACAAGGGAATTTACCTG
TGTGGACACTCAGCCGGGGCCCACCTGGCTGCCATGATGCTCCTGGCCGACTGGACCAAG
CATGGGGTCACGCCCAACCTCAGAGGCTTTTTCCTGGTGAGTGGGGTCTTTGACCTGGAG
CCCATCGTGTATACTTCACAGAACGTTGCTCTCCAGCTGACCCTGGAGGACGCTCAGAGG
AATAGCCCCCAGCTGAAGGTGGCCCAGGCACAGCCGGTGGACCCCACCTGCCGTGTGCTG
GTGGTCGTGGGCCAGTTCGACTCCCCCGAATTCCACCGACAGTCCTGGGAGTTTTACCAG
ACCCTGTGTCAAGGAGAGTGGAAAGCCTCATTTGAAGAGCTCCACGATGTGGACCACTTT
GAAATTGTTGAGAATCTGACCCAGAAGGACAACGTGCTCACCCAGATTATCTTGAAAACA
ATCTTCCAGTAG
Enzyme 3 GenBank Gene ID BC132824 Link Image
Enzyme 3 GeneCard ID A2RUB3 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.3
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