ID 6PGD_SYNE7 Reviewed; 471 AA. AC P21577; Q31S98; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 4. DT 04-NOV-2026, entry version 154. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44 {ECO:0000250|UniProtKB:P00350}; GN Name=gnd; OrderedLocusNames=Synpcc7942_0039; OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Synechococcaceae; Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBSTRATE-BINDING SITE. RX PubMed=2113917; DOI=10.1128/jb.172.7.4023-4031.1990; RA Broedel S.E. Jr., Wolf R.E. Jr.; RT "Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain RT PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase."; RL J. Bacteriol. 172:4023-4031(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Culler D.C., Krogmann D.W.; RT "Amino acid sequence comparisons of 6-phosphogluconate dehydrogenase."; RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Golden S., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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; M55002; AAA27330.1; -; Genomic_DNA. DR EMBL; X58719; CAA41555.1; -; Genomic_DNA. DR EMBL; CP000100; ABB56071.1; -; Genomic_DNA. DR PIR; S14628; S14628. DR RefSeq; WP_011377413.1; NC_007604.1. DR AlphaFoldDB; P21577; -. DR SMR; P21577; -. DR STRING; 1140.Synpcc7942_0039; -. DR PaxDb; 1140-Synpcc7942_0039; -. DR GeneID; 72428848; -. DR KEGG; syf:Synpcc7942_0039; -. DR eggNOG; COG0362; Bacteria. DR HOGENOM; CLU_024540_4_2_3; -. DR OMA; AAAEYNW; -. DR OrthoDB; 9804542at2; -. DR BioCyc; SYNEL:SYNPCC7942_0039-MONOMER; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000889800; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR FunFam; 1.10.1040.10:FF:000002; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR FunFam; 1.20.5.320:FF:000001; 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 1: Evidence at protein level; KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; KW Reference proteome. FT CHAIN 1..471 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090060" FT ACT_SITE 183 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00350" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 33 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 34 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 38 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 75 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 76 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P00350" FT BINDING 103 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P96789" FT BINDING 129 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 130 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 131 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 183 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 187 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 190 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 191 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 263 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 290 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 449 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 455 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 CONFLICT 154..159 FT /note="EPIVRS -> SRSVPT (in Ref. 1; AAA27330)" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="S -> T (in Ref. 2; CAA41555)" FT /evidence="ECO:0000305" FT CONFLICT 407 FT /note="A -> R (in Ref. 2; CAA41555)" FT /evidence="ECO:0000305" FT CONFLICT 415..439 FT /note="AAERGIPVPAFSASLDYFDSYRRDR -> RQNEEFRFRFQCFPGLLRQLPAR FT S (in Ref. 2; CAA41555)" FT /evidence="ECO:0000305" FT CONFLICT 437..441 FT /note="RDRLP -> ASPA (in Ref. 1; AAA27330)" FT /evidence="ECO:0000305" FT CONFLICT 450..453 FT /note="DYFG -> TTC (in Ref. 1; AAA27330)" FT /evidence="ECO:0000305" FT CONFLICT 458..465 FT /note="ERTDRSGS -> KAPIALL (in Ref. 1; AAA27330)" FT /evidence="ECO:0000305" FT CONFLICT 469..470 FT /note="QW -> M (in Ref. 1; AAA27330)" FT /evidence="ECO:0000305" SQ SEQUENCE 471 AA; 51073 MW; 0C75D58209E124E7 CRC64; MALQQFGLIG LAVMGENLAL NIERNGFSLT VYNRTAEKTE AFMADRAQGK NIVPAYSLED FVASLERPRR ILVMVKAGGP VDAVVEQLKP LLDPGDLIID GGNSLFTDTE RRVKDLEALG LGFMGMGVSG GEEGALNGPS LMPGGTQAAY EAVEPIVRSI AAQVDDGPCV TYIGPGGSGH YVKMVHNGIE YGDMQLIAEA YDLLKSVAGL NASELHDVFA AWNKTPELDS FLIEITADIF TKVDDLGTGQ PLVELILDAA GQKGTGRWTV ETALEIGVAI PTIIAAVNAR ILSSIKAERQ AASEILSGPI TEPFSGDRQA FIDSVRDALY CSKICSYAQG MALLAKASQV YNYGLNLGEL ARIWKGGCII RAGFLNKIKQ AYDADPTLAN LLLAPEFRQT ILDRQLAWRR VIAIAAERGI PVPAFSASLD YFDSYRRDRL PQNLTQAQRD YFGAHTYERT DRSGSFHAQW F //