ID A0A1X0WI15_9GAMM Unreviewed; 469 AA. AC A0A1X0WI15; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 25-OCT-2017, entry version 4. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; GN ORFNames=BS640_06090 {ECO:0000313|EMBL:ORJ26409.1}; OS Rouxiella badensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Rouxiella. OX NCBI_TaxID=1646377 {ECO:0000313|EMBL:ORJ26409.1, ECO:0000313|Proteomes:UP000192536}; RN [1] {ECO:0000313|EMBL:ORJ26409.1, ECO:0000313|Proteomes:UP000192536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 100043 {ECO:0000313|EMBL:ORJ26409.1, RC ECO:0000313|Proteomes:UP000192536}; RX PubMed=28100296; RA LE Fleche-Mateos A., Kugler J.H., Hansen S.H., Syldatk C., RA Hausmann R., Lomprez F., Vandenbogaert M., Manuguerra J.C., RA Grimont P.A.; RT "Rouxiella badensis sp. nov. and Rouxiella silvae sp. nov. isolated RT from peat bog soil in Germany and emendation of the genus RT description."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2017). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6- CC phosphogluconate to ribulose 5-phosphate and CO(2), with CC concomitant reduction of NADP to NADPH. CC {ECO:0000256|PIRNR:PIRNR000109}. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. {ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. {ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. {ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ORJ26409.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MRWE01000007; ORJ26409.1; -; Genomic_DNA. DR RefSeq; WP_017490007.1; NZ_MRWE01000007.1. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000192536; Unassembled WGS sequence. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_Gnd/GntZ. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR006183; Pgluconate_DH. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR SMART; SM01350; 6PGD; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000192536}; KW Gluconate utilization {ECO:0000256|RuleBase:RU000485}; KW NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109, KW ECO:0000256|RuleBase:RU000485}; KW Pentose shunt {ECO:0000256|PIRNR:PIRNR000109, KW ECO:0000256|RuleBase:RU000485}. FT DOMAIN 179 468 6PGD. {ECO:0000259|SMART:SM01350}. FT NP_BIND 10 15 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 33 35 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 74 76 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT REGION 128 130 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT REGION 186 187 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT ACT_SITE 183 183 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000109-1}. FT ACT_SITE 190 190 Proton donor. {ECO:0000256|PIRSR: FT PIRSR000109-1}. FT BINDING 102 102 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT BINDING 102 102 Substrate. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT BINDING 191 191 Substrate. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT BINDING 260 260 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 287 287 Substrate. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT BINDING 446 446 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 452 452 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. SQ SEQUENCE 469 AA; 51569 MW; FD3875317566772B CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYSVA IFNRSGDKTD EVVAENPGKN LVPYYTVEEF VESLEKPRRI LLMVKAGEAT DKTIASLTPH LDKGDILIDG GNTFYKDTIR RNKELSDQGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILEQIA ARADDGDACV AYIGADGAGH YVKMVHNGIE YGDMQLIAEA YSLLKQSLNL SNEELATTFA EWNKGELSSY LIDITKDIFT KKDEAGNYLV DVILDEAANK GTGKWTSQSS LDLGEPLTLI TESVFARYLS SLKDQRVAAS KVLTGPAVKA FAGDKAEFIE KIRRALYLGK IVSYAQGFSQ LKAASDENNW NLHYGEIAKI FRAGCIIRAQ FLQKITDAYE ENASIANLLL APYFKNIADE YQQALRDVVS YAVQNGIPTP TFSAAINYYD SYRSAVLPAN LIQAQRDYFG AHTYKRTDKE GVFHTEWLD //