ID G6PD_BUCAP Reviewed; 490 AA. AC Q8K9M2; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 25-NOV-2008, entry version 46. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49; GN Name=zwf; OrderedLocusNames=BUsg_312; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono- CC 1,5-lactone 6-phosphate + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate 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; AE013218; AAM67866.1; -; Genomic_DNA. DR RefSeq; NP_660655.1; -. DR HSSP; P11411; 1DPG. DR GeneID; 1005516; -. DR GenomeReviews; AE013218_GR; BUsg_312. DR KEGG; bas:BUsg312; -. DR HOGENOM; Q8K9M2; -. DR BioCyc; BAPH198804:BUSG312-MON; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001282; Glc-6-P_DHase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR23429; G6PDH; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR ProDom; PD001129; G6PD; 1. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; KW Oxidoreductase. FT CHAIN 1 490 Glucose-6-phosphate 1-dehydrogenase. FT /FTId=PRO_0000068113. FT ACT_SITE 238 238 Proton acceptor (By similarity). FT BINDING 17 17 NADP (By similarity). FT BINDING 49 49 NADP (By similarity). FT BINDING 176 176 Substrate (By similarity). FT BINDING 180 180 Substrate (By similarity). FT BINDING 343 343 Substrate (By similarity). SQ SEQUENCE 490 AA; 57531 MW; 8554072078E042D9 CRC64; MIIETNQACD LVIFGTKGDL ARRKLLPALY KLEKSQKIHP DTRIIGTGRA DWNTEDYIKI VKKAIKMFLN EKIDEKIWKK LRSRLNFFYI DVFQDLHFLE LKNILNQKKN IIIYYCAVPS NTFNAIFTGL GKVNLNSFPS RIIIEKPLGV SLETSKKINN QIAKYFLESQ IFRIDHYLGK ESILNLLALR FSNSFFFHSW NNKIIDHIQI TVSEEVGIEN RWNYFDQMGQ TRDMVQNHLL QILTIVSMDK PKNITPEGIR DEKLKILRSL KKIDLNEIHI KTARGQYASG IINGKKVPSY IEENGANKHS KTETFVSIKV DINNDRWFGV PFYLRTGKRL AYKYSEIVIV FKKISKNLFQ EFNKNLSPNK LIIRLEPNES IKIYFLNKVP GLSKEYKLKS DKMEFNFNIN NTKNFVDAYE RLLFESMRGI QSLFVCREEV EEAWKWIDPI INGWKKTNIN TVQLYKSGTW GPKSSDEIIM RDGRFWETFN //