ID 6PGD_DROSI Reviewed; 481 AA. AC P41573; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 115. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=Pgd; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7240; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=8138153; DOI=10.1093/genetics/136.1.155; RA Begun D.J.; RT "Evolutionary inferences from DNA variation at the 6-phosphogluconate RT dehydrogenase locus in natural populations of Drosophila: selection and RT geographic differentiation."; RL Genetics 136:155-171(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}. 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 -!- 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; U02288; AAA18587.1; -; Unassigned_DNA. DR AlphaFoldDB; P41573; -. DR SMR; P41573; -. DR EnsemblMetazoa; XM_016173312.3; XP_016037778.1; LOC6724920. DR OrthoDB; 434986at2759; -. DR UniPathway; UPA00115; UER00410. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0042593; P:glucose homeostasis; IEA:EnsemblMetazoa. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:EnsemblMetazoa. DR FunFam; 1.10.1040.10:FF:000002; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR FunFam; 1.20.5.320: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..481 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090070" FT ACT_SITE 184 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 191 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 11..16 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 34..36 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 76..78 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 130..132 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 187..188 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 192 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 259 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 286 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250" FT BINDING 445 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" FT BINDING 451 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250" SQ SEQUENCE 481 AA; 52394 MW; 49F97625D5B94822 CRC64; MSGQADIALI GLAVMGQNLI LNMDEKGFVV CAYNRTVAKV KEFLANEAKG TNVIGADSLK DMVSKLKSPR KVMLLVKGGS AVDDFIQQLV PLLSAGDVII DGGNSEYQDT SRRCDELAKL GLLYVGSGVS GGEEGARHGP SLMPGGHEAA WPLIQPIFQA ICAKADGEPC CEWVGDGGAG HFVKMVHNGI EYGDMQLICE AYHIMQSLGL SADQMADEFG KWNSAELDSF LIEITRDILK YKDGKGHLLE RIRDTAGQKG TGKWTAIAAL QYGVPVTLIG EAVFSRCLSA LKDERVQASS VLKGPSTKAE VANLTKFLDD IKHALYCAKI VSYAQGFMLM REAARENKWR LNYGGIALMW RGGCIIRSVF LGNIKDAYTS QPQLSNLLLD DFFKKAIERG QDSWREVVAN AFRWGIPVPA LSTALSFYDG YRTAKLPANL LQAQRDYFGA HTYELLGQEG QFHHTNWTGT GGNVSASTYQ A //