ID G6PD_NOSP7 Reviewed; 509 AA. AC P48848; B2J6J9; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 04-NOV-2026, entry version 128. 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}; GN OrderedLocusNames=Npun_F4025; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales; OC Nostocaceae; Nostoc. OX NCBI_TaxID=63737; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7870816; DOI=10.1104/pp.107.1.267; RA Summers M.L., Meeks J.C., Chu S., Wolf R.E. Jr.; RT "Nucleotide sequence of an operon in Nostoc sp. strain ATCC 29133 encoding RT four genes of the oxidative pentose phosphate cycle."; RL Plant Physiol. 107:267-268(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102; RX PubMed=23463784; DOI=10.1104/pp.112.213116; RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.; RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a RT Cyanobacterium-Plant Symbiosis."; RL Plant Physiol. 161:1984-1992(2013). 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 + NADPH + H(+); 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; L32796; AAA50770.1; -; Genomic_DNA. DR EMBL; CP001037; ACC82404.1; -; Genomic_DNA. DR RefSeq; WP_012410371.1; NC_010628.1. DR AlphaFoldDB; P48848; -. DR SMR; P48848; -. DR STRING; 63737.Npun_F4025; -. DR EnsemblBacteria; ACC82404; ACC82404; Npun_F4025. DR KEGG; npu:Npun_F4025; -. DR eggNOG; COG0364; Bacteria. DR HOGENOM; CLU_013524_5_0_3; -. DR OMA; AACLQYM; -. DR OrthoDB; 9802739at2; -. DR PhylomeDB; P48848; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000001191; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:InterPro. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. 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..509 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068130" FT ACT_SITE 259 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 62 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 104..105 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 167 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 197 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 201 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 235 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 359 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 364 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" SQ SEQUENCE 509 AA; 58268 MW; 7FA3196A3199A8AA CRC64; MVSLLENPLR VGLQQQGMPE PQIIVIFGAS GDLTWRKLVP ALYKLRRERR IPPETTIVGV ARREWSHEYF REQMQKGMEE AHPDVDLGEL WQDFSQGLFY SPGDIDNPES YQKLKTLLSE LDEKRGTRGN RMFYLSVAPS FFPEAIKQLG SGGMLEDPYK HRLVIEKPFG RDLASAQSLN QVVQKYCKEH QVYRIDHYLG KETVQNLLVF RFANAIFEPL WNRQFVDHVQ ITVAETVGVE DRAGYYESAG ALRDMLQNHL MQLYCLTAME APNAMDADSI RTEKVKVLQA TRLADVHNLS RSAVRGQYSA GWMKGQAVPG YRTEPGVDPN STTPTYVAMK FLVDNWRWKG VPFYLRTGKR MPKKVSEIAI HFREVPSRMF QSAAQQTNAN ILTMRIQPNE GISLRFDVKM PGAEFRTRSV DMDFSYGSFG IQATSDAYDR LFLDCMMGDQ TLFTRADEVE AAWQVVTPAL SVWDAPADPT TIPQYEAGTW EPEQAELLIN QDGRRWRRL //