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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 - DNA adducts
  • 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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  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  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 ]