CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005069
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 4-aminobutyrate aminotransferase GabT 
Protein Synonyms/Alias
 (S)-3-amino-2-methylpropionate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT 
Gene Name
 gabT 
Gene Synonyms/Alias
 b2662; JW2637 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
71AAVEAQLKKLSHTCFacetylation[1]
151YTLALTGKVNPYSAGacetylation[1]
192ASIHRIFKNDAAPEDacetylation[1, 2]
323EQENLLQKANDLGQKacetylation[1]
330KANDLGQKLKDGLLAacetylation[1]
341GLLAIAEKHPEIGDVacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
Functional Description
 Catalyzes the transfer of the amino group from gamma- aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). 
Sequence Annotation
 REGION 111 112 Pyridoxal phosphate binding.
 REGION 239 242 Pyridoxal phosphate binding.
 BINDING 138 138 Pyridoxal phosphate.
 BINDING 297 297 Pyridoxal phosphate.
 MOD_RES 268 268 N6-(pyridoxal phosphate)lysine.  
Keyword
 3D-structure; Aminotransferase; Complete proteome; Direct protein sequencing; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 426 AA 
Protein Sequence
MNSNKELMQR RSQAIPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI AVLNTGHLHP 60
KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD FAKKTLLVTT GSEAVENAVK 120
IARAATKRSG TIAFSGAYHG RTHYTLALTG KVNPYSAGMG LMPGHVYRAL YPCPLHGISE 180
DDAIASIHRI FKNDAAPEDI AAIVIEPVQG EGGFYASSPA FMQRLRALCD EHGIMLIADE 240
VQSGAGRTGT LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG 300
NPIACVAALE VLKVFEQENL LQKANDLGQK LKDGLLAIAE KHPEIGDVRG LGAMIAIELF 360
EDGDHNKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL VPLTIEDAQI RQGLEIISQC 420
FDEAKQ 426 
Gene Ontology
 GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:EC.
 GO:0003867; F:4-aminobutyrate transaminase activity; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
 GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:EcoCyc. 
Interpro
 IPR004632; 4NH2But_aminotransferase_bac.
 IPR005814; Aminotrans_3.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00202; Aminotran_3 
SMART
  
PROSITE
 PS00600; AA_TRANSFER_CLASS_3 
PRINTS