CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001743
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 6-phosphogluconate dehydrogenase, decarboxylating 
Protein Synonyms/Alias
  
Gene Name
 gnd 
Gene Synonyms/Alias
 b2029; JW2011 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
38IFNRSREKTEEVIAEacetylation[1, 2]
49VIAENPGKKLVPYYTacetylation[2]
50IAENPGKKLVPYYTVacetylation[1, 2]
58LVPYYTVKEFVESLEacetylation[1, 2]
75RRILLMVKAGAGTDAacetylation[1]
88DAAIDSLKPYLDKGDacetylation[2]
93SLKPYLDKGDIIIDGacetylation[2]
136GGEEGALKGPSIMPGacetylation[2]
146SIMPGGQKEAYELVAacetylation[2]
158LVAPILTKIAAVAEDacetylation[1]
242TKDIFTKKDEDGNYLacetylation[2]
260ILDEAANKGTGKWTSacetylation[1, 2]
264AANKGTGKWTSQSALacetylation[1, 2]
301DQRVAASKVLSGPQAacetylation[1, 2]
314QAQPAGDKAEFIEKVacetylation[2]
320DKAEFIEKVRRALYLacetylation[1, 2]
358LNYGEIAKIFRAGCIacetylation[2]
454YFGAHTYKRIDKEGVacetylation[1, 2]
458HTYKRIDKEGVFHTEacetylation[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
 Catalyzes the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. 
Sequence Annotation
 NP_BIND 10 15 NADP.
 NP_BIND 33 35 NADP.
 NP_BIND 74 76 NADP.
 REGION 128 130 Substrate binding.
 REGION 186 187 Substrate binding (By similarity).
 ACT_SITE 183 183 Proton acceptor.
 ACT_SITE 190 190 Proton donor.
 BINDING 102 102 NADP (By similarity).
 BINDING 102 102 Substrate.
 BINDING 191 191 Substrate (By similarity).
 BINDING 260 260 Substrate; via amide nitrogen.
 BINDING 287 287 Substrate.
 BINDING 445 445 Substrate; shared with dimeric partner.
 BINDING 451 451 Substrate; shared with dimeric partner.  
Keyword
 3D-structure; Complete proteome; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 468 AA 
Protein Sequence
MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LVPYYTVKEF 60
VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF 120
NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH 180
YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL TNEELAQTFT EWNNGELSSY LIDITKDIFT 240
KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS 300
KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF 360
RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT 420
FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD 468 
Gene Ontology
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IDA:UniProtKB.
 GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
 GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB. 
Interpro
 IPR008927; 6-PGluconate_DH_C-like.
 IPR006114; 6PGDH_C.
 IPR006113; 6PGDH_decarbox.
 IPR006115; 6PGDH_NADP-bd.
 IPR006184; 6PGdom_BS.
 IPR013328; DH_multihelical.
 IPR012284; Fibritin/6PGD_C-extension.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF00393; 6PGD
 PF03446; NAD_binding_2 
SMART
  
PROSITE
 PS00461; 6PGD 
PRINTS