CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003146
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate-pyruvate aminotransferase AlaA 
Protein Synonyms/Alias
  
Gene Name
 alaA 
Gene Synonyms/Alias
 yfbQ; b2290; JW2287 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
262NGPKKHAKGYIEGLEacetylation[1]
337GALYMFPKIDAKRFNacetylation[1]
350FNIHDDQKMVLDFLLacetylation[1]
394DIELSLSKFARFLSGacetylation[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
 Involved in the biosynthesis of alanine. 
Sequence Annotation
 BINDING 41 41 Substrate; via amide nitrogen (By
 BINDING 179 179 Substrate (By similarity).
 BINDING 378 378 Substrate (By similarity).
 MOD_RES 240 240 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 405 AA 
Protein Sequence
MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA PDEILVDVIR 60
NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI GNGVSELIVQ AMQALLNSGD 120
EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE SSDWFPDLDD IRAKITPRTR GIVIINPNNP 180
TGAVYSKELL MEIVEIARQH NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK 240
TYRVAGFRQG WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI 300
TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA KRFNIHDDQK MVLDFLLQEK 360
VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS GYHQL 405 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0030632; P:D-alanine biosynthetic process; IMP:UniProtKB.
 GO:0019272; P:L-alanine biosynthetic process from pyruvate; IMP:EcoCyc.
 GO:0046677; P:response to antibiotic; IMP:EcoCyc.
 GO:0006974; P:response to DNA damage stimulus; IMP:EcoCyc. 
Interpro
 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
 PS00105; AA_TRANSFER_CLASS_1 
PRINTS