ID 6PGD_CAEEL Reviewed; 484 AA. AC Q17761; Q22772; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 2. DT 27-MAR-2024, entry version 151. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN ORFNames=T25B9.9; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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}. 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 -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. 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; Z70311; CAA94380.1; -; Genomic_DNA. DR EMBL; Z70306; CAA94380.1; JOINED; Genomic_DNA. DR PIR; T19020; T19020. DR RefSeq; NP_501998.1; NM_069597.5. DR AlphaFoldDB; Q17761; -. DR SMR; Q17761; -. DR BioGRID; 43072; 21. DR STRING; 6239.T25B9.9.1; -. DR EPD; Q17761; -. DR PaxDb; 6239-T25B9-9; -. DR PeptideAtlas; Q17761; -. DR EnsemblMetazoa; T25B9.9.1; T25B9.9.1; WBGene00012015. DR GeneID; 177971; -. DR KEGG; cel:CELE_T25B9.9; -. DR UCSC; T25B9.9.1; c. elegans. DR AGR; WB:WBGene00012015; -. DR WormBase; T25B9.9; CE06508; WBGene00012015; -. DR eggNOG; KOG2653; Eukaryota. DR GeneTree; ENSGT00390000009023; -. DR HOGENOM; CLU_024540_4_2_1; -. DR InParanoid; Q17761; -. DR OMA; CVTHVGP; -. DR OrthoDB; 3013545at2759; -. DR PhylomeDB; Q17761; -. DR Reactome; R-CEL-71336; Pentose phosphate pathway. DR UniPathway; UPA00115; UER00410. DR PRO; PR:Q17761; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00012015; Expressed in adult organism and 4 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IBA:GO_Central. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IBA:GO_Central. DR GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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 PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1. DR PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 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; KW Reference proteome. FT CHAIN 1..484 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090067" FT ACT_SITE 183 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 10..15 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 33..35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 75..77 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 129..131 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 186..187 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 191 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 287 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 448 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 454 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" SQ SEQUENCE 484 AA; 53196 MW; D3CF6F1065F17535 CRC64; MAEADIAVIG LAVMGQNLIL NMNDHGFTVC AFNRTVKLVD DFLANEAKGT KIIGAHSIEE MCKKLKRPRR VMMLIKAGTP VDMMIDAIVP HLEEGDIIID GGNSEYTDSN RRSEQLAAKG IMFVGCGVSG GEEGARFGPS LMPGGNPKAW PHLKDIFQKI AAKSNGEPCC DWVGNAGSGH FVKMVHNGIE YGDMQLIAEA YHLLSKAVEL NHDQMAEVLD DWNKGELESF LIEITANILK YRDEQGEPIV PKIRDSAGQK GTGKWTCFAA LEYGLPVTLI GEAVFARCLS ALKDERVRAS KQLPRPQVSP DTVVQDKRVF IKQISKALYA SKIVSYAQGF MLLAEASKQF NWNLNFGAIA LMWRGGCIIR SRFLGDIEHA FQKNKQLSNL LLDDFFTKAI TEAQDSWRVV VCAAVRLGIP VPAFSSALAF YDGYTSEVVP ANLLQAQRDY FGAHTYELLA KPGTWVHTNW TGTGGRVTSN AYNA //