CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003326
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glucose-6-phosphate 1-dehydrogenase 
Protein Synonyms/Alias
 G6PD; Extracellular death factor; EDF 
Gene Name
 zwf 
Gene Synonyms/Alias
 b1852; JW1841 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
25KGDLARRKLLPSLYQacetylation[1, 2]
35PSLYQLEKAGQLNPDacetylation[2]
55VGRADWDKAAYTKVVacetylation[2]
60WDKAAYTKVVREALEacetylation[2]
71EALETFMKETIDEGLacetylation[2]
109LGAMLDQKNRITINYacetylation[2]
135CKGLGEAKLNAKPARacetylation[2]
139GEAKLNAKPARVVMEacetylation[1, 2]
147PARVVMEKPLGTSLAacetylation[2]
181RIDHYLGKETVLNLLacetylation[2]
228GRWGYFDKAGQMRDMacetylation[2]
296TAGFAQGKKVPGYLEacetylation[2]
309LEEEGANKSSNTETFacetylation[2]
344TGKRLPTKCSEVVVYacetylation[2]
361TPELNLFKESWQDLPacetylation[2]
396KVPGLDHKHNLQITKacetylation[2]
403KHNLQITKLDLSYSEacetylation[2]
Reference
 [1] 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]
 [2] 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
  
Sequence Annotation
 ACT_SITE 239 239 Proton acceptor (By similarity).
 BINDING 18 18 NADP (By similarity).
 BINDING 50 50 NADP (By similarity).
 BINDING 177 177 Substrate (By similarity).
 BINDING 181 181 Substrate (By similarity).
 BINDING 344 344 Substrate (By similarity).  
Keyword
 Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; Oxidoreductase; Quorum sensing; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 491 AA 
Protein Sequence
MAVTQTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGQLN PDTRIIGVGR ADWDKAAYTK 60
VVREALETFM KETIDEGLWD TLSARLDFCN LDVNDTAAFS RLGAMLDQKN RITINYFAMP 120
PSTFGAICKG LGEAKLNAKP ARVVMEKPLG TSLATSQEIN DQVGEYFEEC QVYRIDHYLG 180
KETVLNLLAL RFANSLFVNN WDNRTIDHVE ITVAEEVGIE GRWGYFDKAG QMRDMIQNHL 240
LQILCMIAMS PPSDLSADSI RDEKVKVLKS LRRIDRSNVR EKTVRGQYTA GFAQGKKVPG 300
YLEEEGANKS SNTETFVAIR VDIDNWRWAG VPFYLRTGKR LPTKCSEVVV YFKTPELNLF 360
KESWQDLPQN KLTIRLQPDE GVDIQVLNKV PGLDHKHNLQ ITKLDLSYSE TFNQTHLADA 420
YERLLLETMR GIQALFVRRD EVEEAWKWVD SITEAWAMDN DAPKPYQAGT WGPVASVAMI 480
TRDGRSWNEF E 491 
Gene Ontology
 GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IMP:EcoliWiki.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
 GO:0009372; P:quorum sensing; IEA:UniProtKB-KW. 
Interpro
 IPR001282; G6P_DH.
 IPR019796; G6P_DH_AS.
 IPR022675; G6P_DH_C.
 IPR022674; G6P_DH_NAD-bd.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF02781; G6PD_C
 PF00479; G6PD_N 
SMART
  
PROSITE
 PS00069; G6P_DEHYDROGENASE 
PRINTS
 PR00079; G6PDHDRGNASE.