ID A0A0D8KBB9_9RHIZ Unreviewed; 491 AA. AC A0A0D8KBB9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 22-JUL-2015, entry version 3. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00966, ECO:0000256|RuleBase:RU000497}; DE Short=G6PD {ECO:0000256|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000256|HAMAP-Rule:MF_00966, ECO:0000256|RuleBase:RU000497}; GN Name=zwf {ECO:0000256|HAMAP-Rule:MF_00966}; GN ORFNames=RS75_15660 {ECO:0000313|EMBL:KJF66842.1}; OS Rhizobium nepotum 39/7. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1368418 {ECO:0000313|EMBL:KJF66842.1}; RN [1] {ECO:0000313|EMBL:KJF66842.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=39/7 {ECO:0000313|EMBL:KJF66842.1}; RA Kuzmanovic N., Pulawska J., Obradovic A.; RT "Draft Genome Sequences of Agrobacterium nepotum Strain 39/7T (= CFBP RT 7436T = LMG 26435T) and Agrobacterium sp. Strain KFB 330 (= CFBP 8308 RT = LMG 28674)."; RL Submitted (MAR-2015) 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: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- CC glucono-1,5-lactone + NADPH. {ECO:0000256|HAMAP-Rule:MF_00966, CC ECO:0000256|RuleBase:RU000497}. 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 ECO:0000256|RuleBase:RU000497}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00966, CC ECO:0000256|RuleBase:RU000497}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJF66842.1}. 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; JWJH01000014; KJF66842.1; -; Genomic_DNA. DR RefSeq; WP_045021959.1; NZ_JWJH01000014.1. DR UniPathway; UPA00115; UER00408. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom. 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 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 ECO:0000256|RuleBase:RU000497}; KW Glucose metabolism {ECO:0000256|HAMAP-Rule:MF_00966, KW ECO:0000256|RuleBase:RU000497}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00966, ECO:0000256|RuleBase:RU000497}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00966, KW ECO:0000256|RuleBase:RU000497}. FT ACT_SITE 242 242 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 51 51 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT BINDING 150 150 NADP. {ECO:0000256|HAMAP-Rule:MF_00966}. FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 184 184 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 218 218 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 237 237 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. FT BINDING 341 341 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00966}. SQ SEQUENCE 491 AA; 54978 MW; D7AB33A314C20A17 CRC64; MSSQIIPVEA FDCVVFGGTG DLAERKLLPA LYHRQVEGQF TEPTRIIGAS RSVMTHEEYR KFAQDALKEH LKAGEYDDAQ VALFLNRIFY VPVDAKSGNG WDLLKKLLDE GKERIRAFYL AVAPGIFGDI ADKIREHKLI TRSTRIVVEK PIGRDLASAQ ILNDTIGHVF KEEQIFRIDH YLGKETVQNL MALRFANALY EPLWNSAHID HVQITVAEAV GLEGRAGYYD KAGALRDMVQ NHILQLLCLV AMEPPASMNA EAVRDEKLKV LRSLKRIDTS NVEKLTVRGQ YRAGASAGGP VKGYLEELEG GVSNTETFVA IKAEIANWRW AGVPFYIRTG KRLATRVSEI VVTFKQIPHS IFDDAAGKIE ANKLVIRLQP DEGVKQSLLI KDPGPGGMRL RQVSLDMSFA EAFNVRSPDA YERLLMDTIR SNQTLFMRRD EVEAAWDWVD PILKSWEDLA QGVQGYTAGT WGPSGSIALI ERDGRTWHDA D //