ID 6PGD_PSEVU Reviewed; 445 AA. AC P41574; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 04-NOV-2026, entry version 112. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44 {ECO:0000250|UniProtKB:P00350}; DE Flags: Fragment; GN Name=gnd; OS Pseudescherichia vulneris (Escherichia vulneris). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Pseudescherichia. OX NCBI_TaxID=566; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33821 / DSM 4564 / JCM 1688 / BCRC 15953 / CCUG 15715 / RC LMG 7868 / NBRC 102420 / NCTC 12130 / CDC 875-72 / NIH 580; RX PubMed=7937867; DOI=10.1073/pnas.91.21.10227; RA Nelson K., Selander R.K.; RT "Intergeneric transfer and recombination of the 6-phosphogluconate RT dehydrogenase gene (gnd) in enteric bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10227-10231(1994). 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:0000250|UniProtKB:P00350}. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2 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:0000250|UniProtKB:P00350}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 3/3. {ECO:0000250|UniProtKB:P00350}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00350}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family. CC {ECO:0000305}. 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; U14465; AAC43815.1; -; Genomic_DNA. DR AlphaFoldDB; P41574; -. DR SMR; P41574; -. DR UniPathway; UPA00115; UER00410. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB. DR GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB. DR FunFam; 1.10.1040.10:FF:000002; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR FunFam; 3.40.50.720:FF:000007; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00873; gnd; 1. DR NCBIfam; NF006765; gndA; 1. DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN <1..>445 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090039" FT ACT_SITE 172 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00350" FT ACT_SITE 179 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 3 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 22 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 23 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 24 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 27 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 63 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 64 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 91 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 117 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 118 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 119 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 172 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 176 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 179 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 180 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 249 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 276 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 434 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 440 FT /ligand="6-phospho-D-gluconate" FT /ligand_id="ChEBI:CHEBI:58759" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P00350" FT NON_TER 1 FT NON_TER 445 SQ SEQUENCE 445 AA; 48806 MW; 0315BE126C2A45FE CRC64; AVMGRNLALN IESRGYTVSV FNRSREKTEE VVAENPGKKL VPYYTVQEFV ESLETPRRIL LMVQAGAGTD AAINSLKPYL DKGDIIIDGG NTFFHDTIRR NRELSAEGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILTKIAA VAEDGEPCVT YIGADGAGHY VKMVHNGIEY GDMQLIAEAY SLLKGGLNLS NEELAQTFTE WNKGELSSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKEQRVAASK VLSGPQSQPA GDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASEEYNWDL NYGEIAKIFR AGCIIRAQFL QKITDAYAET PAIANLLLAP YFKQIADDYQ QALRDVVAYA VQNGIPVPTF GAAVAYYDSY RAAVLPANLI QAQRDYFGAH TYKRT //