ID F9URG7_LACPL Unreviewed; 494 AA. AC F9URG7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 25-OCT-2017, entry version 46. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00966}; DE Short=G6PD {ECO:0000256|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000256|HAMAP-Rule:MF_00966}; GN Name=gpd {ECO:0000313|EMBL:CCC79806.1}; GN Synonyms=zwf {ECO:0000256|HAMAP-Rule:MF_00966}; GN OrderedLocusNames=lp_2681 {ECO:0000313|EMBL:CCC79806.1}; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC79806.1, ECO:0000313|Proteomes:UP000000432}; RN [1] {ECO:0000313|EMBL:CCC79806.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] {ECO:0000313|EMBL:CCC79806.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; RX PubMed=22156394; DOI=10.1128/JB.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- CC phosphogluconolactone. {ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- CC glucono-1,5-lactone + NADPH. {ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. {ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00966}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL935263; CCC79806.1; -; Genomic_DNA. DR RefSeq; WP_003644713.1; NC_004567.2. DR RefSeq; YP_004890320.1; NC_004567.2. DR ProteinModelPortal; F9URG7; -. DR STRING; 220668.lp_2681; -. DR EnsemblBacteria; CCC79806; CCC79806; lp_2681. DR GeneID; 1062946; -. DR KEGG; lpl:lp_2681; -. DR PATRIC; fig|220668.9.peg.2245; -. DR eggNOG; ENOG4105D8W; Bacteria. DR eggNOG; COG0364; LUCA. DR KO; K00036; -. DR OMA; VEICVYE; -. DR BioCyc; LPLA220668:G137Z-2287-MONOMER; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR23429; PTHR23429; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00966}; KW Complete proteome {ECO:0000313|Proteomes:UP000000432}; KW Glucose metabolism {ECO:0000256|HAMAP-Rule:MF_00966}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00966}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00966, KW ECO:0000313|EMBL:CCC79806.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000432}. FT DOMAIN 11 188 G6PD_N. {ECO:0000259|Pfam:PF00479}. FT DOMAIN 191 490 G6PD_C. {ECO:0000259|Pfam:PF02781}. FT NP_BIND 86 87 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT ACT_SITE 241 241 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 47 47 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT BINDING 149 149 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT BINDING 179 179 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 183 183 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 217 217 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 236 236 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 337 337 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 342 342 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. SQ SEQUENCE 494 AA; 56786 MW; 46018F265C3BFA56 CRC64; MSNEKIALFT IFGGTGDLAQ RKLYPSLFKL YQKGYLKDHF AVIGTARRPW TDDHYHEVIS DSLADLNADQ ETVTQFASHF YYQSHDVTDA EHYRTLKKLS EKLDAQYGLQ GNRIFYLAMA PNFFGTIAQH LRSENILTDN GFNRVIIEKP FGHDYESAKE LNDQLTATFN ENQIYRIDHY LGKEMIQNIT AIRFGNNIWE SLWNNRYIDN VQITLSEKLG VEERAVYYDN SGALRDMVQN HILQILSLLT MDQPVEFTEN DIDVEKVKAL RSLRPLKPEE VATNFVRGQY GAGDDAKAYR DEDKISSDSN TDTFVAGKVM IDNYRWSGVP FYIRTGKRLA DKFTRIDVVF KRPVVNIFNH EDVRANDDAA TSLDPNILTI NVEPTEGFEL RMNAKAIGQG FATTPVKLNY SHDAEATAGS PEAYERLLHD ALNGDATNFT HWQEVADSWK FVDVIQKYWD EHQPEFPNYR PGTMGPDAAD ELLRQDGHRW VYRN //