Canmetcon
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Identification
HMDB Protein ID HMDBP00464
Secondary Accession Numbers
  • 5703
  • HMDBP03656
Name Kynurenine--oxoglutarate transaminase 1
Synonyms
  1. Cysteine-S-conjugate beta-lyase
  2. GTK
  3. Glutamine transaminase K
  4. Glutamine--phenylpyruvate transaminase
  5. KATI
  6. Kynurenine aminotransferase I
  7. Kynurenine--oxoglutarate transaminase I
Gene Name CCBL1
Protein Type Enzyme
Biological Properties
General Function Involved in 1-aminocyclopropane-1-carboxylate synthase activity
Specific Function Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.
Pathways
  • Chemical carcinogenesis
  • L-kynurenine degradation
  • Selenocompound metabolism
  • Tryptophan metabolism
Reactions
L-Kynurenine + Oxoglutaric acid → 4-(2-Aminophenyl)-2,4-dioxobutanoic acid + L-Glutamic acid details
L-Glutamine + Phenylpyruvic acid → 2-Keto-glutaramic acid + L-Phenylalanine details
RS-CH(2)-CH(NH(3)(+))COO(-) + Water → RSH + Ammonia + Pyruvic acid details
L-3-Hydroxykynurenine + Oxoglutaric acid → 4-(2-Amino-3-hydroxyphenyl)-2,4-dioxobutanoic acid + L-Glutamic acid details
Se-Methylselenocysteine + 2-Oxo-4-methylthiobutanoic acid → Methylselenopyruvate + L-Methionine details
GO Classification
Biological Process
tryptophan catabolic process
cellular amino acid biosynthetic process
L-kynurenine catabolic process
L-phenylalanine catabolic process
Cellular Component
cytosol
nucleus
Function
carbon-sulfur lyase activity
1-aminocyclopropane-1-carboxylate synthase activity
binding
catalytic activity
transferase activity
lyase activity
transferase activity, transferring nitrogenous groups
cofactor binding
pyridoxal phosphate binding
Molecular Function
kynurenine-oxoglutarate transaminase activity
pyridoxal phosphate binding
cysteine-S-conjugate beta-lyase activity
glutamine-phenylpyruvate transaminase activity
L-glutamine:pyruvate aminotransferase activity
L-phenylalanine-oxaloacetate transaminase activity
L-phenylalanine:pyruvate aminotransferase activity
Process
metabolic process
biosynthetic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 9
Locus 9q34.11
SNPs CCBL1
Gene Sequence
>1269 bp
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTCATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
Protein Properties
Number of Residues 422
Molecular Weight 47874.765
Theoretical pI 6.473
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Kynurenine--oxoglutarate transaminase 1
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
GenBank ID Protein 758591
UniProtKB/Swiss-Prot ID Q16773
UniProtKB/Swiss-Prot Entry Name KAT1_HUMAN
PDB IDs
GenBank Gene ID X82224
GeneCard ID CCBL1
GenAtlas ID CCBL1
HGNC ID HGNC:1564
References
General References
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  3. Perry S, Harries H, Scholfield C, Lock T, King L, Gibson G, Goldfarb P: Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase. FEBS Lett. 1995 Mar 6;360(3):277-80. [PubMed:7883047 ]
  4. Rossi F, Han Q, Li J, Li J, Rizzi M: Crystal structure of human kynurenine aminotransferase I. J Biol Chem. 2004 Nov 26;279(48):50214-20. Epub 2004 Sep 10. [PubMed:15364907 ]
  5. Han Q, Robinson H, Cai T, Tagle DA, Li J: Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem. 2009 May 14;52(9):2786-93. doi: 10.1021/jm9000874. [PubMed:19338303 ]