ID G6PD_THEMA Reviewed; 496 AA. AC Q9X0N9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 138. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966}; DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966}; GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=TM_1155; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- CC phosphogluconolactone. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family. CC {ECO:0000255|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; AE000512; AAD36231.1; -; Genomic_DNA. DR PIR; G72289; G72289. DR RefSeq; NP_228961.1; NC_000853.1. DR RefSeq; WP_004080226.1; NZ_CP011107.1. DR AlphaFoldDB; Q9X0N9; -. DR SMR; Q9X0N9; -. DR STRING; 243274.TM_1155; -. DR PaxDb; 243274-THEMA_08565; -. DR EnsemblBacteria; AAD36231; AAD36231; TM_1155. DR KEGG; tma:TM1155; -. DR eggNOG; COG0364; Bacteria. DR InParanoid; Q9X0N9; -. DR OrthoDB; 9802739at2; -. DR SABIO-RK; Q9X0N9; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central. 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; Glucose metabolism; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..496 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068136" FT ACT_SITE 245 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 31..38 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 65 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 153 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 221 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 240 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 345 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 350 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" SQ SEQUENCE 496 AA; 57536 MW; 572106FCE08F20E8 CRC64; MKCSLGLEKC PDDTLRCFPK IEQPFGIVIF GASGDLTKRK LIPALNRLFE AGILPERFFV LGAARTKMDD KKFRSRFDAN PDFLEHCSYI SVDYQDPESF KQLKNTIETL IKRIDSSNLV FYLAVPPDLY IPILENLSKT GLNEKPARVV IEKPFGKDLE SARRLEDTLQ KYFQEDQIFR IDHYLGKETV QNILVFRFAN FIFEEIWNNK FVDHVQITMA EDIGVEHRAG YFENVGLLRD IFQNHMLQIL ALIAMEPPSS FNGENFRNER VKLLRSIRPF PVEELESWIV RGQYGRGVVN GKEVPAYREE PGVAKDSNVE TFVAMKLFID NWRWSGVPFY LRSGKRLPKK ITEVAVVFKK IPHSIFAGVP SDELEPNTIV FTLQPNEGIS LEFQVKRPCP GMFPQLLSMD FRYEDYFGVK LPDAYERLLL DVILGDPTLF MRRDDLEVSW ELLDPVLKAW ENDPVRFSPY VYPAGTWGPR EADLLIERDG RKWRKL //