ID A0A8B5QX69_LEUME Unreviewed; 486 AA. AC A0A8B5QX69; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. 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 ORFNames=FEZ47_07350 {ECO:0000313|EMBL:TLP94940.1}; OS Leuconostoc mesenteroides. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Leuconostoc. OX NCBI_TaxID=1245 {ECO:0000313|EMBL:TLP94940.1, ECO:0000313|Proteomes:UP000307918}; RN [1] {ECO:0000313|EMBL:TLP94940.1, ECO:0000313|Proteomes:UP000307918} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FAM 18356 {ECO:0000313|EMBL:TLP94940.1, RC ECO:0000313|Proteomes:UP000307918}; RA Roder T., Wuthrich D., Sattari Z., Von Ah U., Bar C., Ronchi F., RA Macpherson A.J., Ganal-Vonarburg S.C., Bruggmann R., Vergeres G.; RT "The metagenome of a microbial culture collection derived from dairy RT environment covers the genomic content of the human microbiome."; RL Submitted (MAY-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TLP94940.1}. 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; VBTD01000011; TLP94940.1; -; Genomic_DNA. DR RefSeq; WP_050892019.1; NZ_VBTD01000011.1. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000307918; Unassembled WGS sequence. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. 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|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}. 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 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; 54576 MW; 726009B0AFAED404 CRC64; MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQEHF AIVGTARQQL SDDEFKQLVR DSIKDFTEDQ AQAEAFIAHF SYRAHDVTDA ASYGILKSAI EEAATKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLAET GYNRLMIEKP FGTSYATAEE LQSDLENAFD DDQLFRIDHY LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLAEVLG VEERAGYYDT TGALLDMIQN HTMQIVGWLA MEKPESFNDK DIRAAKNAAF NALKIYNEEE VNKYFVRAQY GAGDTADYKP YLEEADVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKAGTFNFG SEQEAQESVL SIIIDPKGAI ELKLNAKSVE DAFNTRTINL DWAVSDEDKK NTPEPYERMI HDTMNGDGSN FADWNGVSIA WKFVDAITAV YDADEAPLET YKSGSMGPEA SDKLLAENGD AWVFKG //