ID 6PGD_SYNE7 Reviewed; 471 AA. AC P21577; Q31S98; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 4. DT 25-NOV-2008, entry version 61. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=Synpcc7942_0039; OS Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBSTRATE-BINDING SITE. RX MEDLINE=90299831; PubMed=2113917; RA Broedel S.E. Jr., Wolf R.E. Jr.; RT "Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. RT strain PCC 7942 gene (gnd) encoding 6-phosphogluconate RT dehydrogenase."; RL J. Bacteriol. 172:4023-4031(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Culler D.C., Krogmann D.W.; RT "Amino acid sequence comparisons of 6-phosphogluconate RT dehydrogenase."; RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC RT 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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; M55002; AAA27330.1; -; Genomic_DNA. DR EMBL; X58719; CAA41555.1; -; Genomic_DNA. DR EMBL; CP000100; ABB56071.1; -; Genomic_DNA. DR PIR; S14628; S14628. DR RefSeq; YP_399058.1; -. DR HSSP; P00349; 2PGD. DR GeneID; 3775852; -. DR GenomeReviews; CP000100_GR; Synpcc7942_0039. DR KEGG; syf:Synpcc7942_0039; -. DR HOGENOM; P21577; -. DR BioCyc; SELO1140:SYNPCC7942_0039-MON; -. 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 1: Evidence at protein level; KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 471 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090060. FT CONFLICT 154 159 EPIVRS -> SRSVPT (in Ref. 1; AAA27330). FT CONFLICT 159 159 S -> T (in Ref. 2; CAA41555). FT CONFLICT 407 407 A -> R (in Ref. 2; CAA41555). FT CONFLICT 415 439 AAERGIPVPAFSASLDYFDSYRRDR -> RQNEEFRFRFQC FT FPGLLRQLPARS (in Ref. 2; CAA41555). FT CONFLICT 437 441 RDRLP -> ASPA (in Ref. 1; AAA27330). FT CONFLICT 450 453 DYFG -> TTC (in Ref. 1). FT CONFLICT 458 465 ERTDRSGS -> KAPIALL (in Ref. 1; FT AAA27330). FT CONFLICT 469 470 QW -> M (in Ref. 1). SQ SEQUENCE 471 AA; 51073 MW; 0C75D58209E124E7 CRC64; MALQQFGLIG LAVMGENLAL NIERNGFSLT VYNRTAEKTE AFMADRAQGK NIVPAYSLED FVASLERPRR ILVMVKAGGP VDAVVEQLKP LLDPGDLIID GGNSLFTDTE RRVKDLEALG LGFMGMGVSG GEEGALNGPS LMPGGTQAAY EAVEPIVRSI AAQVDDGPCV TYIGPGGSGH YVKMVHNGIE YGDMQLIAEA YDLLKSVAGL NASELHDVFA AWNKTPELDS FLIEITADIF TKVDDLGTGQ PLVELILDAA GQKGTGRWTV ETALEIGVAI PTIIAAVNAR ILSSIKAERQ AASEILSGPI TEPFSGDRQA FIDSVRDALY CSKICSYAQG MALLAKASQV YNYGLNLGEL ARIWKGGCII RAGFLNKIKQ AYDADPTLAN LLLAPEFRQT ILDRQLAWRR VIAIAAERGI PVPAFSASLD YFDSYRRDRL PQNLTQAQRD YFGAHTYERT DRSGSFHAQW F //