ID G6PD_NOSS1 Reviewed; 509 AA. AC P48992; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 02-SEP-2026, entry version 139. 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=all4019; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales; OC Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8566707; DOI=10.1111/j.1574-6968.1995.tb07882.x; RA Newman J., Karakaya H., Scanlan D.J., Mann N.H.; RT "A comparison of gene organization in the zwf region of the genomes of the RT cyanobacteria Synechococcus sp. PCC 7942 and Anabaena sp. PCC 7120."; RL FEMS Microbiol. Lett. 133:187-193(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., RA Takazawa M., Yamada M., Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). 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; U33282; AAA98853.1; -; Genomic_DNA. DR EMBL; BA000019; BAB75718.1; -; Genomic_DNA. DR PIR; AD2308; AD2308. DR RefSeq; WP_010998159.1; NC_003272.1. DR AlphaFoldDB; P48992; -. DR SMR; P48992; -. DR STRING; 103690.gene:10496062; -. DR KEGG; ana:all4019; -. DR eggNOG; COG0364; Bacteria. DR OrthoDB; 9802739at2; -. DR SABIO-RK; P48992; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000002483; 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_0000068109" 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" FT CONFLICT 417 FT /note="T -> S (in Ref. 1; AAA98853)" FT /evidence="ECO:0000305" SQ SEQUENCE 509 AA; 58304 MW; FEC3CFBF7119E977 CRC64; MVSLLENPLR VGLQQQGMPE PQIIVIFGAS GDLTWRKLVP ALYKLRRERR IPPETTIVGV ARREWSHEYF REQMQKGMEE AHSSVELGEL WQDFSQGLFY CPGDIDNPES YQKLKNLLSE LDEKRGTRGN RMFYLSVAPN FFPEAIKQLG GAGMLDDPYK HRLVIEKPFG RDLASAQSLN AVVQKYCKEH QVYRIDHYLG KETVQNLLVF RFANAIFEPL WNRQFVDHVQ ITVAETVGVE DRAGYYEKAG ALRDMLQNHL MQLYCLTAME APNSMDADSI RTEKVKVLQA TRLADVHNLS RSAIRGQYSA GWMKGQQVPG YRTEPGVDPN SSTPTYVGMK FLVDNWRWQG VPFYLRTGKR MPKKVSEISI HFRDVPSRMF QSAAQQRNAN ILAMRIQPNE GISLRFDVKM PGAEFRTRSV DMDFSYGSFG IEATSDAYDR LFLDCMMGDQ TLFTRADEVE AAWQVVTPAL SVWDSPADPA TIPQYEAGTW EPAEAEFLIN QDGRRWRRL //