CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008294
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 4-aminobutyrate aminotransferase PuuE 
Protein Synonyms/Alias
 GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase 
Gene Name
 puuE 
Gene Synonyms/Alias
 goaG; b1302; JW1295 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
191DAIERLFKSDIEAKQacetylation[1]
338KNTLIDAKESVPAIAacetylation[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] 
Functional Description
 Catalyzes the transfer of the amino group from gamma- aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). PuuE is important for utilization of putrescine as the sole nitrogen or carbon source. 
Sequence Annotation
 REGION 110 111 Pyridoxal phosphate binding (By
 REGION 238 241 Pyridoxal phosphate binding (By
 BINDING 296 296 Pyridoxal phosphate (By similarity).
 MOD_RES 267 267 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Aminotransferase; Complete proteome; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 421 AA 
Protein Sequence
MSNNEFHQRR LSATPRGVGV MCNFFAQSAE NATLKDVEGN EYIDFAAGIA VLNTGHRHPD 60
LVAAVEQQLQ QFTHTAYQIV PYESYVTLAE KINALAPVSG QAKTAFFTTG AEAVENAVKI 120
ARAHTGRPGV IAFSGGFHGR TYMTMALTGK VAPYKIGFGP FPGSVYHVPY PSDLHGISTQ 180
DSLDAIERLF KSDIEAKQVA AIIFEPVQGE GGFNVAPKEL VAAIRRLCDE HGIVMIADEV 240
QSGFARTGKL FAMDHYADKP DLMTMAKSLA GGMPLSGVVG NANIMDAPAP GGLGGTYAGN 300
PLAVAAAHAV LNIIDKESLC ERANQLGQRL KNTLIDAKES VPAIAAVRGL GSMIAVEFND 360
PQTGEPSAAI AQKIQQRALA QGLLLLTCGA YGNVIRFLYP LTIPDAQFDA AMKILQDALS 420
D 421 
Gene Ontology
 GO:0003867; F:4-aminobutyrate transaminase activity; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
 GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
 GO:0009447; P:putrescine 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