ID 6PGD_KLETE Reviewed; 445 AA. AC P41577; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 109. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44 {ECO:0000250|UniProtKB:P00350}; DE Flags: Fragment; GN Name=gnd; OS Klebsiella terrigena (Raoultella terrigena). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33257 / DSM 2687 / JCM 1687 / NBRC 14941 / NCTC 13038 / RC VTT-E-97854; 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; U14473; AAC43819.1; -; Genomic_DNA. DR AlphaFoldDB; P41577; -. DR SMR; P41577; -. 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; PRK09287.1; 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_0000090044" 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; 48834 MW; 2FBD0E46CDAB69A8 CRC64; AVMGRNLALN IESRGYTVSV FNRSREKTEE VIAENPGKKL VPHYTVKEFV ESLETPRRIL LMVKAGAGTD SAIDSLKPYL DKGDIIIDGG NTFFQDTIRR NRELSADGFN FIGTGVSGGE EGALKGPSIM PGGQKEAYEL VAPILEQIAA RAEDGEPCVA YIGADGAGHY VKMVHNGIEY GDMQLIAEAY ALLKGGLALS NEELATTFTE WNQGELSSYL IDITKDIFTK KDEEGKYLVD VILDEAANKG TGKWTSQSSL DLGEPLSLIT ESVFARYISS LKDQRVAASK VLTGPQAQPA SDKAEFIEKV RRALYLGKIV SYAQGFSQLR AASNEYSWDL NYGEIAKIFR AGCIIRAQFL QKITDAYEEN AGIANLLLAP YFKQIADEYQ QALRDVVAYA VQNGIPVPTF SAAIAYYDSY RSAVLPANLI QAQRDYFGAH TYKRT //