ID A0A2U3MQY6_LEUCA Unreviewed; 486 AA. AC A0A2U3MQY6; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 07-APR-2021, entry version 10. 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=zwf {ECO:0000256|HAMAP-Rule:MF_00966, GN ECO:0000313|EMBL:SPJ43645.1}; GN ORFNames=LCAC16_270115 {ECO:0000313|EMBL:SPJ43645.1}; OS Leuconostoc carnosum. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=1252 {ECO:0000313|EMBL:SPJ43645.1, ECO:0000313|Proteomes:UP000295336}; RN [1] {ECO:0000313|Proteomes:UP000295336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MFPC16A2803 {ECO:0000313|Proteomes:UP000295336}; RA Chaillou S.; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. 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|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family. CC {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; ONZM01000020; SPJ43645.1; -; Genomic_DNA. DR EnsemblBacteria; SPJ43645; SPJ43645; LCAC16_270115. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000295336; Unassembled WGS sequence. 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 Coiled coil {ECO:0000256|SAM:Coils}; 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}. FT DOMAIN 11..188 FT /note="G6PD_N" FT /evidence="ECO:0000259|Pfam:PF00479" FT DOMAIN 191..482 FT /note="G6PD_C" FT /evidence="ECO:0000259|Pfam:PF02781" FT NP_BIND 13..20 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT NP_BIND 86..87 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT COILED 158..178 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 241 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 47 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 149 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 179 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 183 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966, FT ECO:0000256|PROSITE-ProRule:PRU10005" FT BINDING 217 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 236 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 339 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 344 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" SQ SEQUENCE 486 AA; 54803 MW; F7B2D454B1C475C3 CRC64; MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQNL TDDEFKQLVR ESIADFTDDK SQAEEFITHF SYRAHDVTDA ASYGILKEAI EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLAST GYNRLMIEKP FGTSYDKAEE LQRDLENAFD DNQLFRIDHY LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN HTMQIVGWLA MEKPESFNDK DIRAAKNAAF NALKIYNEEE VNKYFVRAQY GAGDSAAFKP YLEEMDVPAD SKNNTFMAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKSGTFNFG TEQEAQEAVL SIIIDPKGAI DFKINSKSVE DAFNTRMINL DWTVSDEDKQ NTPEPYERMI HDTMNGDGSN FADWNGVSIA WKFVDAISDV YAADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG //