ID G6PD_SYNE7 Reviewed; 511 AA. AC P29686; Q31KQ5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 2. DT 27-MAR-2024, entry version 135. 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=Synpcc7942_2334; OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1643289; DOI=10.1007/bf00027085; RA Scanlan D.J., Newman J., Sebaihia M., Mann N.H., Carr N.G.; RT "Cloning and sequence analysis of the glucose-6-phosphate dehydrogenase RT gene from the cyanobacterium Synechococcus PCC 7942."; RL Plant Mol. Biol. 19:877-880(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33912 / PCC 7942 / FACHB-805; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Golden S., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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; U33285; AAA98847.1; -; Genomic_DNA. DR EMBL; CP000100; ABB58364.1; -; Genomic_DNA. DR PIR; S23520; DEYCG6. DR RefSeq; WP_011244078.1; NZ_JACJTX010000001.1. DR AlphaFoldDB; P29686; -. DR SMR; P29686; -. DR STRING; 1140.Synpcc7942_2334; -. DR PaxDb; 1140-Synpcc7942_2334; -. DR GeneID; 76401065; -. DR KEGG; syf:Synpcc7942_2334; -. DR eggNOG; COG0364; Bacteria. DR HOGENOM; CLU_013524_5_0_3; -. DR OrthoDB; 9802739at2; -. DR BioCyc; SYNEL:SYNPCC7942_2334-MONOMER; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000889800; Chromosome. 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 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..511 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068134" FT ACT_SITE 260 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 63 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 168 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 202 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 236 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 365 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT CONFLICT 506..511 FT /note="RRWRRL -> AVGVVSRIPATQLNSSGDV (in Ref. 1)" FT /evidence="ECO:0000305" SQ SEQUENCE 511 AA; 58095 MW; 9F16062520B51B10 CRC64; MTPKLLENPL RIGLRQDKVP EPQILVIFGA TGDLTQRKLV PAIYEMHLER RLPPELTIVG VARRDWSDDY FREHLRQGVE QFGGGIQAEE VWNTFAQGLF FAPGNIDDPQ FYQTLRDRLA NLDELRGTRG NRTFYLSVAP RFFGEAAKQL GAAGMLADPA KTRLVVEKPF GRDLSSAQVL NAILQNVCRE SQIYRIDHYL GKETVQNLLV FRFANAIFEP LWNRQYIDHV QITVAETVGL EGRAGYYETA GALRDMVQNH LMQLFSLTAM EPPNSLGADG IRNEKVKVVQ ATRLADIDDL SLSAVRGQYK AGWMNGRSVP AYRDEEGADP QSFTPTYVAM KLLVDNWRWQ GVPFYLRTGK RMPKKVTEIA IQFKTVPHLM FQSATQKVNS PNVLVLRIQP NEGVSLRFEV KTPGSSQRTR SVDMDFRYDT AFGSPTQEAY SRLLVDCMLG DQTLFTRADE VEASWRVVTP LLESWDDPRQ AAGISFYEAG TWEPAEAEQL INRDGRRWRR L //