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 25-NOV-2008, entry version 50. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=Pgd; OS Ceratitis capitata (Mediterranean fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Tephritoidea; Tephritidae; Ceratitis; Ceratitis. OX NCBI_TaxID=7213; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94093871; PubMed=8269100; RX 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 RT glucose-6-phosphate dehydrogenase from the mediterranean fruit fly RT Ceratitis capitata: correlating genetic and physical maps of RT chromosome 5."; RL Insect Mol. Biol. 1:213-222(1993). CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S67873; AAB29396.1; -; mRNA. DR HSSP; P00349; 2PGD. DR SMR; P41570; 3-472. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IEA:InterPro. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR InterPro; IPR006183; 6-phosphogluconate_DHase. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NAD-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR013328; DHase_multihelical. DR InterPro; IPR012284; Fibritin/6PGD_C-extension. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 2: Evidence at transcript level; KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 481 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090068. 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 //