ID A0A1X0WI15_9GAMM Unreviewed; 469 AA. AC A0A1X0WI15; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 12-OCT-2022, entry version 20. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|ARBA:ARBA00018193, ECO:0000256|PIRNR:PIRNR000109}; DE EC=1.1.1.44 {ECO:0000256|ARBA:ARBA00013011, ECO:0000256|PIRNR:PIRNR000109}; 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; DOI=10.1099/ijsem.0.001794; RA Le Fleche-Mateos A., Kugler J.H., Hansen S.H., Syldatk C., Hausmann R., RA Lomprez F., Vandenbogaert M., Manuguerra J.C., Grimont P.A.; RT "Rouxiella badensis sp. nov. and Rouxiella silvae sp. nov. isolated from RT peat bog soil in Germany and emendation of the genus description."; RL Int. J. Syst. Evol. Microbiol. 67:1255-1259(2017). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP CC to NADPH. {ECO:0000256|ARBA:ARBA00002526, CC ECO:0000256|PIRNR:PIRNR000109}. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44; CC Evidence={ECO:0000256|ARBA:ARBA00000530, CC ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 3/3. {ECO:0000256|ARBA:ARBA00004874, ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, CC ECO:0000256|PIRNR:PIRNR000109}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 STRING; 1646377.BS640_06090; -. DR EnsemblBacteria; ORJ26409; ORJ26409; BS640_06090. DR GeneID; 68686043; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000192536; Unassembled WGS sequence. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. 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:0016054; P:organic acid catabolic process; IEA:UniProt. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. 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 PANTHER; PTHR11811; PTHR11811; 1. 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 Gluconate utilization {ECO:0000256|ARBA:ARBA00023064, KW ECO:0000256|RuleBase:RU000485}; KW NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000109}; KW Pentose shunt {ECO:0000256|PIRNR:PIRNR000109, KW ECO:0000256|RuleBase:RU000485}; KW Reference proteome {ECO:0000313|Proteomes:UP000192536}. FT DOMAIN 179..468 FT /note="6PGD" FT /evidence="ECO:0000259|SMART:SM01350" FT ACT_SITE 183 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1" FT BINDING 10..15 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 33..35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 74..76 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 102 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 102 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 128..130 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 186..187 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 191 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 260 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 287 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 446 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 452 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="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 //