Tag | Content |
---|
CPLM ID | CPLM-010475 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 6-phosphogluconate dehydrogenase, NADP(+)-dependent, decarboxylating |
Protein Synonyms/Alias | GNTZII |
Gene Name | gndA |
Gene Synonyms/Alias | yqjI; BSU23860 |
Created Date | July 27, 2013 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Lysine Modification | Position | Peptide | Type | References |
---|
93 | SLLPHLEKDDILIDG | acetylation | [1] | 106 | DGGNTYYKDTQRRNK | acetylation | [1] | 309 | LLSGPEVKPVTENKE | acetylation | [1] | 459 | HTYERTDKEGIFHTE | acetylation | [1] |
|
Reference | [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG. Proteomics. 2013 May;13(10-11):1726-36. [ PMID: 23468065] |
Functional Description | Catalyzes the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Is the predominant 6-P- gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate. |
Sequence Annotation | NP_BIND 10 15 NADP (By similarity). NP_BIND 33 35 NADP (By similarity). NP_BIND 74 76 NADP (By similarity). REGION 128 130 Substrate binding (By similarity). REGION 185 186 Substrate binding (By similarity). ACT_SITE 182 182 Proton acceptor (By similarity). ACT_SITE 189 189 Proton donor (By similarity). BINDING 102 102 NADP (By similarity). BINDING 102 102 Substrate (By similarity). BINDING 190 190 Substrate (By similarity). BINDING 260 260 Substrate; via amide nitrogen (By BINDING 287 287 Substrate (By similarity). BINDING 446 446 Substrate; shared with dimeric partner BINDING 452 452 Substrate; shared with dimeric partner |
Keyword | Complete proteome; Direct protein sequencing; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 469 AA |
Protein Sequence | MSKQQIGVIG LAVMGKNLAL NIESRGFSVS VYNRSSSKTE EFLQEAKGKN VVGTYSIEEF 60 VQSLETPRKI LLMVKAGTAT DATIQSLLPH LEKDDILIDG GNTYYKDTQR RNKELAESGI 120 HFIGTGVSGG EEGALKGPSI MPGGQKEAHE LVKPILEAIS AKVDGEPCTT YIGPDGAGHY 180 VKMVHNGIEY GDMQLISESY FILKQVLGLS ADELHEVFAE WNKGELDSYL IEITADIFTK 240 KDEETGKPLV DVILDKAGQK GTGKWTSQSA LDLGVPLPII TESVFARFIS AMKEERVKAS 300 GLLSGPEVKP VTENKEELIE AVRKALFMSK ICSYAQGFAQ MKAASEEYNW DLKYGEIAMI 360 FRGGCIIRAA FLQKIKEAYD REPELDNLLL DSYFKNIVES YQGALRQVIS LAVAQGVPVP 420 SFSSALAYYD SYRTAVLPAN LIQAQRDYFG AHTYERTDKE GIFHTEWMK 469 |
Gene Ontology | GO:0050661; F:NADP binding; IEA:InterPro. GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:EC. GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |