ID G6PD_BACSU Reviewed; 489 AA. AC P54547; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 25-NOV-2008, entry version 65. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49; DE AltName: Full=Vegetative protein 11; DE Short=VEG11; GN Name=zwf; Synonyms=yqjJ; OrderedLocusNames=BSU23850; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / JH642; RX MEDLINE=97124195; PubMed=8969508; RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., RA Kobayashi Y.; RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of RT the Bacillus subtilis genome containing the skin element and many RT sporulation genes."; RL Microbiology 142:3103-3111(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP PROTEIN SEQUENCE OF 1-15. RC STRAIN=168 / IS58; RX MEDLINE=97443988; PubMed=9298659; DOI=10.1002/elps.1150180820; RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.; RT "First steps from a two-dimensional protein index towards a response- RT regulation map for Bacillus subtilis."; RL Electrophoresis 18:1451-1463(1997). 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; D84432; BAA12616.1; -; Genomic_DNA. DR EMBL; Z99116; CAB14317.1; -; Genomic_DNA. DR PIR; B69964; B69964. DR RefSeq; NP_390266.1; -. DR HSSP; P11411; 1DPG. DR GeneID; 938690; -. DR GenomeReviews; AL009126_GR; BSU23850. DR KEGG; bsu:BSU23850; -. DR NMPDR; fig|224308.1.peg.2390; -. DR SubtiList; BG11739; zwf. DR HOGENOM; P54547; -. DR BioCyc; BSUB224308:BSU2384-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 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Direct protein sequencing; KW Glucose metabolism; NADP; Oxidoreductase. FT CHAIN 1 489 Glucose-6-phosphate 1-dehydrogenase. FT /FTId=PRO_0000068110. FT ACT_SITE 241 241 Proton acceptor (By similarity). FT BINDING 17 17 NADP (By similarity). FT BINDING 49 49 NADP (By similarity). FT BINDING 179 179 Substrate (By similarity). FT BINDING 183 183 Substrate (By similarity). FT BINDING 346 346 Substrate (By similarity). SQ SEQUENCE 489 AA; 55660 MW; 4994B670EBFFF191 CRC64; MKTNQQPKAV IVIFGATGDL AKRKLYPSIH RLYQNGQIGE EFAVVGVGRR PWSNEDLRQT VKTSISSSAD KHIDDFTSHF YYHPFDVTNP GSYQELNVLL NQLEDTYQIP NNRMFYLAMA PEFFGTIAKT LKSEGVTATT GWSRLVIEKP FGHDLPSAQA LNKEIREAFT EDQIYRIDHY LGKQMVQNIE VIRFANAIFE PLWTNRYISN IQITSSESLG VEDRARYYEK SGALRDMVQN HIMQMVALLA MEPPIKLNTE EIRSEKVKVL RALRPIAKDE VDEYFVRGQY HAGEIDGVPV PAYTDEDNVA PDSNTETFVA GKLLIDNFRW AGVPFYIRTG KRMREKSTKI VVQFKDIPMN LYYGNENNMN PNLLVIHIQP DEGITLYLNA KKLGGAAHAQ PIKLDYCSNC NDELNTPEAY EKLIHDCLLG DATNFAHWDE VALSWSFVDS ISETWAANKT LSPNYESGSM GPKESDDLLV KDGLHWWNI //