ID 6PGD_CERCA Reviewed; 481 AA. AC P41570; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-SEP-2023, entry version 104. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=Pgd; OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea; OC Tephritidae; Ceratitis; Ceratitis. OX NCBI_TaxID=7213; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8269100; DOI=10.1111/j.1365-2583.1993.tb00094.x; RA Scott M.J., Kriticou D., Robinson A.S.; RT "Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and glucose- RT 6-phosphate dehydrogenase from the mediterranean fruit fly Ceratitis RT capitata: correlating genetic and physical maps of chromosome 5."; RL Insect Mol. Biol. 1:213-222(1993). 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; S67873; AAB29396.1; -; mRNA. DR RefSeq; NP_001266319.1; NM_001279390.1. DR AlphaFoldDB; P41570; -. DR SMR; P41570; -. DR EnsemblMetazoa; NM_001279390.1; NP_001266319.1; LOC101451876. DR GeneID; 101451876; -. DR KEGG; ccat:101451876; -. DR OrthoDB; 3013545at2759; -. 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:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. 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 2: Evidence at transcript level; KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1..481 FT /note="6-phosphogluconate dehydrogenase, decarboxylating" FT /id="PRO_0000090068" 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; 52964 MW; F0ABB506AD1B86D0 CRC64; MSAKADIALI GLAVMGQNLV LNMNDKGFVV CAYNRTVEKV NQFLKNEAKG TNVIGATSLQ DMVNKLKLPR KIMLLVKAGS AVDDFIQQLV PLLSPGDVII DGGNSEYQDT ARRCDELRAK KILYVGSGVS GGEEGARHGP SLMPGGHPEA WPLIQPIFQS ICAKADKEPC CEWVGEGGAG HFVKMVHNGI EYGDMQLICE AYQIMKALGL SQAEMATEFE KWNSEELDSF LIEITRDILN YQDDRGYLLE RIRDTAGQKG TGKWTAISAL QYGVPVTLIG EAVFSRCLSA LKDERVAASK QLKGPNVNAK VEDLPKFLNH IKHALYCSKI VSYAQGFMLM REAAKENNWN LNYGGIALMW RGGCIIRSVF LGNIKDAYTR NPQLSNLLLD DFFKKAIEVG QNSWRQVVAN AFLWGIPVPA LSTALSFYDG YRTEKLPANL LQAQRDYFGA HTYELLGAEG KFVHTNWTGT GGNVSASTYQ A //