ID 6PGD9_ECOLX Reviewed; 468 AA. AC P37754; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 25-NOV-2008, entry version 51. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=O9:K30:H12 / E69; RX MEDLINE=94252978; PubMed=7515042; RA Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., RA Whitfield C.; RT "Cloning and analysis of duplicated rfbM and rfbK genes involved in RT the formation of GDP-mannose in Escherichia coli O9:K30 and RT participation of rfb genes in the synthesis of the group I K30 RT capsular polysaccharide."; RL J. Bacteriol. 176:3126-3139(1994). 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; L27646; AAA21136.1; -; Genomic_DNA. DR PIR; I41250; I41250. DR HSSP; P00349; 2PGD. 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 3: Inferred from homology; KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090038. SQ SEQUENCE 468 AA; 51625 MW; C13D94CFD78BFF3A CRC64; MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK LVPYYTVQEF VESLETPRRI LLMVKAGSGT DSAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILKQIA AVAEDGEPCV TYIGADGAGH YVKMVHNGIE YGDMQLIAEA YALLKGGLTL SNEELAQTFT EWNEGELSSY LYDITKDIFT KKDEEGKYLV DVILDEAANK GTGKWTSQSS LDLGEPLSLI TESVFPRYIS SLKDQRVAAS KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYNWE LNYAEIAKIF RAGCIIRAQF LQKITDAYAQ NAGIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIRVPT FSAAIAYYDS YRSAVLPANL IQAQRDYFGA HTYKRTDKEG VFHTEWLE //