Tag | Content |
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CPLM ID | CPLM-017457 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial |
Protein Synonyms/Alias | KAT/AadAT; 2-aminoadipate aminotransferase; 2-aminoadipate transaminase; Alpha-aminoadipate aminotransferase; AadAT; Kynurenine aminotransferase II; Kynurenine--oxoglutarate aminotransferase II; Kynurenine--oxoglutarate transaminase 2; Kynurenine--oxoglutarate transaminase II |
Gene Name | AADAT |
Gene Synonyms/Alias | KAT2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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31 | DILSRGPKSMISLAG | acetylation | [1] | 49 | NPNMFPFKTAVITVE | acetylation | [1] |
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Reference | [1] Regulation of cellular metabolism by protein lysine acetylation. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Science. 2010 Feb 19;327(5968):1000-4. [ PMID: 20167786] |
Functional Description | Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino- group acceptors, with a preference for 2-oxoglutarate, 2- oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro). |
Sequence Annotation | BINDING 20 20 Substrate. BINDING 74 74 Substrate. BINDING 142 142 Substrate. BINDING 202 202 Substrate. BINDING 399 399 Substrate. MOD_RES 263 263 N6-(pyridoxal phosphate)lysine. |
Keyword | 3D-structure; Alternative splicing; Aminotransferase; Complete proteome; Mitochondrion; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 425 AA |
Protein Sequence | MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT AVITVENGKT 60 IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI HYPPSQGQMD LCVTSGSQQG 120 LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH PLGCNIINVA SDESGIVPDS LRDILSRWKP 180 EDAKNPQKNT PKFLYTVPNG NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK 240 FRVPTFLSMD VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ 300 LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP AAGMFLWIKV 360 KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA SFSSASPEQM DVAFQVLAQL 420 IKESL 425 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; TAS:Reactome. GO:0047536; F:2-aminoadipate transaminase activity; IDA:UniProtKB. GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB. GO:0030170; F:pyridoxal phosphate binding; IEA:Compara. GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB. GO:0009058; P:biosynthetic process; IEA:InterPro. GO:0006536; P:glutamate metabolic process; IDA:UniProtKB. GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. GO:0006554; P:lysine catabolic process; TAS:Reactome. GO:0006569; P:tryptophan catabolic process; TAS:Reactome. GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:Compara. |
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