ID F9URG7_LACPL Unreviewed; 494 AA. AC F9URG7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 02-OCT-2024, entry version 70. 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 Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. 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., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W., RA Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R., RA de Vries M., Ursing B., 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: CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5- CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00966}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000256|ARBA:ARBA00004937, ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|HAMAP-Rule:MF_00966}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 AlphaFoldDB; F9URG7; -. DR STRING; 220668.lp_2681; -. DR EnsemblBacteria; CCC79806; CCC79806; lp_2681. DR GeneID; 79829929; -. DR KEGG; lpl:lp_2681; -. DR PATRIC; fig|220668.9.peg.2245; -. DR eggNOG; COG0364; Bacteria. DR HOGENOM; CLU_013524_5_0_9; -. DR OrthoDB; 9802739at2; -. DR PhylomeDB; F9URG7; -. 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR00871; zwf; 1. DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1. DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00966}; KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526, ECO:0000256|HAMAP- KW Rule:MF_00966}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00966}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00966}; Reference proteome {ECO:0000313|Proteomes:UP000000432}. FT DOMAIN 11..188 FT /note="Glucose-6-phosphate dehydrogenase NAD-binding" FT /evidence="ECO:0000259|Pfam:PF00479" FT DOMAIN 191..490 FT /note="Glucose-6-phosphate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02781" FT ACT_SITE 241 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 47 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 86..87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 149 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 179 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 217 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 236 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 337 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 342 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule: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 //