CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009922
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate decarboxylase beta 
Protein Synonyms/Alias
 GAD-beta 
Gene Name
 gadB 
Gene Synonyms/Alias
 b1493; JW1488 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
3*****MDKKQVTDLRacetylation[1]
4****MDKKQVTDLRSacetylation[1]
21LDSRFGAKSISTIAEacetylation[1]
30ISTIAESKRFPLHEMacetylation[1, 2]
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
 Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. 
Sequence Annotation
 REGION 126 127 Pyridoxal phosphate binding.
 BINDING 62 62 Substrate.
 BINDING 83 83 Substrate.
 BINDING 212 212 Pyridoxal phosphate.
 BINDING 275 275 Pyridoxal phosphate.
 MOD_RES 276 276 N6-(pyridoxal phosphate)lysine.
 MOD_RES 446 446 N6-acetyllysine.
 MOD_RES 453 453 N6-acetyllysine.
 MOD_RES 464 464 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Decarboxylase; Direct protein sequencing; Lyase; Membrane; Pyridoxal phosphate; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 466 AA 
Protein Sequence
MDKKQVTDLR SELLDSRFGA KSISTIAESK RFPLHEMRDD VAFQIINDEL YLDGNARQNL 60
ATFCQTWDDE NVHKLMDLSI NKNWIDKEEY PQSAAIDLRC VNMVADLWHA PAPKNGQAVG 120
TNTIGSSEAC MLGGMAMKWR WRKRMEAAGK PTDKPNLVCG PVQICWHKFA RYWDVELREI 180
PMRPGQLFMD PKRMIEACDE NTIGVVPTFG VTYTGNYEFP QPLHDALDKF QADTGIDIDM 240
HIDAASGGFL APFVAPDIVW DFRLPRVKSI SASGHKFGLA PLGCGWVIWR DEEALPQELV 300
FNVDYLGGQI GTFAINFSRP AGQVIAQYYE FLRLGREGYT KVQNASYQVA AYLADEIAKL 360
GPYEFICTGR PDEGIPAVCF KLKDGEDPGY TLYDLSERLR LRGWQVPAFT LGGEATDIVV 420
MRIMCRRGFE MDFAELLLED YKASLKYLSD HPKLQGIAQQ NSFKHT 466 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004351; F:glutamate decarboxylase activity; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006536; P:glutamate metabolic process; IEA:InterPro.
 GO:0051454; P:intracellular pH elevation; IMP:EcoCyc. 
Interpro
 IPR010107; Glutamate_decarboxylase.
 IPR002129; PyrdxlP-dep_de-COase.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR021115; Pyridoxal-P_BS. 
Pfam
 PF00282; Pyridoxal_deC 
SMART
  
PROSITE
 PS00392; DDC_GAD_HDC_YDC 
PRINTS