ID A0A2U3MQY6_LEUCA Unreviewed; 486 AA. AC A0A2U3MQY6; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 05-DEC-2018, entry version 5. 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}; RN [1] {ECO:0000313|EMBL:SPJ43645.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MFPC16A2803 {ECO:0000313|EMBL:SPJ43645.1}; RA Keele B.F.; 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- CC 1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; CC Evidence={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 --------------------------------------------------------------------------- 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 UniPathway; UPA00115; UER00408. 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|HAMAP-Rule:MF_00966}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00966}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00966, KW ECO:0000313|EMBL:SPJ43645.1}. FT DOMAIN 11 188 G6PD_N. {ECO:0000259|Pfam:PF00479}. FT DOMAIN 191 482 G6PD_C. {ECO:0000259|Pfam:PF02781}. FT NP_BIND 13 20 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT NP_BIND 86 87 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT COILED 158 178 {ECO:0000256|SAM:Coils}. 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, ECO:0000256|PROSITE-ProRule: FT PRU10005}. 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 339 339 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 344 344 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //