Tag | Content |
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CPLM ID | CPLM-013518 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Kynurenine--oxoglutarate transaminase 3 |
Protein Synonyms/Alias | Cysteine-S-conjugate beta-lyase 2; Kynurenine aminotransferase III; KATIII; Kynurenine--glyoxylate transaminase; Kynurenine--oxoglutarate transaminase III |
Gene Name | Ccbl2 |
Gene Synonyms/Alias | Kat3 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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187 | SKRTDGMKWTSSDWT | acetylation | [1] | 203 | NPQELESKFSSKTKA | acetylation | [1] | 280 | LTIGSAGKTFSVTGW | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze 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 (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2- oxoglutarate as amino group acceptor (in vitro) (By similarity). |
Sequence Annotation | BINDING 53 53 Substrate (By similarity). BINDING 71 71 Substrate; via amide nitrogen (By BINDING 218 218 Substrate (By similarity). BINDING 429 429 Substrate (By similarity). MOD_RES 116 116 N6-acetyllysine (By similarity). MOD_RES 280 280 N6-(pyridoxal phosphate)lysine (By |
Keyword | Acetylation; Aminotransferase; Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 454 AA |
Protein Sequence | MLLAQRRLFS LGCRAKPIKT IYSSKVLGLS TSAKMALRFK NAKRIEGLDQ NVWVEFTKLA 60 ADPSVVNLGQ GFPDITLPSY VQEELSKAAF IDNLNQYTRG FGHPSLVKAL SCLYGKIYQK 120 QIDPNEEILV TVGGYGSLFN AIQGLVDPGD EVIIMVPFYD CYEPMVKMAG AVPVFIPLRS 180 KRTDGMKWTS SDWTFNPQEL ESKFSSKTKA IILNTPHNPI GKVYTREELQ VIADLCIKHD 240 TLCISDEVYE WLVYTGHKHI KVASLPGMWD RTLTIGSAGK TFSVTGWKLG WSIGPGHLIK 300 HLRTVQQTSV YTCATPLQAA LAEAFWIDIK RMDDPECYFN SLPKELEVKR DRMACLLNSV 360 GLKPIIPDGG YFIIADVSSL GVDLSDVKSD EPYDYKFVKW MTKNKKLSAI PVSAFCDSES 420 KPHFEKLVRF CFIKKDSTLD AAEEIFRTWN SRKS 454 |
Gene Ontology | GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:EC. GO:0047315; F:kynurenine-glyoxylate transaminase activity; ISS:UniProtKB. GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB. GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. GO:0009058; P:biosynthetic process; IEA:InterPro. |
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