ID A0A0D8KBB9_9RHIZ Unreviewed; 491 AA. AC A0A0D8KBB9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 02-DEC-2020, entry version 18. 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=RS75_15660 {ECO:0000313|EMBL:KJF66842.1}; OS Rhizobium nepotum 39/7. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; OC Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1368418 {ECO:0000313|EMBL:KJF66842.1, ECO:0000313|Proteomes:UP000052068}; RN [1] {ECO:0000313|EMBL:KJF66842.1, ECO:0000313|Proteomes:UP000052068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=39/7 {ECO:0000313|EMBL:KJF66842.1, RC ECO:0000313|Proteomes:UP000052068}; RA Kuzmanovic N., Pulawska J., Obradovic A.; RT "Draft Genome Sequences of Agrobacterium nepotum Strain 39/7T (= CFBP 7436T RT = LMG 26435T) and Agrobacterium sp. Strain KFB 330 (= CFBP 8308 = LMG RT 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: 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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: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 EnsemblBacteria; KJF66842; KJF66842; RS75_15660. DR PATRIC; fig|1368418.3.peg.1135; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000052068; 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 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, ECO:0000313|EMBL:KJF66842.1}. FT DOMAIN 14..189 FT /note="G6PD_N" FT /evidence="ECO:0000259|Pfam:PF00479" FT DOMAIN 191..488 FT /note="G6PD_C" FT /evidence="ECO:0000259|Pfam:PF02781" FT ACT_SITE 242 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 51 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 150 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 180 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 184 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966, FT ECO:0000256|PROSITE-ProRule:PRU10005" FT BINDING 218 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 237 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00966" FT BINDING 341 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule: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 //