ID G6PD_SOLTU Reviewed; 511 AA. AC P37830; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 24-JAN-2024, entry version 121. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000269|PubMed:8180621}; GN Name=G6PDH; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, AND PATHWAY. RC STRAIN=cv. Desiree; TISSUE=Green leaf; RX PubMed=8180621; DOI=10.1111/j.1365-313x.1994.00353.x; RA Graeve K., von Schaewen A., Scheibe R.; RT "Purification, characterization, and cDNA sequence of glucose-6-phosphate RT dehydrogenase from potato (Solanum tuberosum L.)."; RL Plant J. 5:353-361(1994). CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose- CC phosphate pathway, which represents a route for the dissimilation of CC carbohydrates besides glycolysis. The main function of this enzyme is CC to generate NADPH for reductive biosyntheses. CC {ECO:0000269|PubMed:8180621}. 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; CC Evidence={ECO:0000269|PubMed:8180621}; CC -!- ACTIVITY REGULATION: Regulated by metabolites. CC {ECO:0000269|PubMed:8180621}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000269|PubMed:8180621}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11413}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11413}. CC -!- TISSUE SPECIFICITY: Found in tubers, stolons, roots, and flower buds. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family. CC {ECO:0000305}. 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; X74421; CAA52442.1; -; mRNA. DR PIR; S60287; S60287. DR AlphaFoldDB; P37830; -. DR SMR; P37830; -. DR STRING; 4113.P37830; -. DR PaxDb; 4113-PGSC0003DMT400052250; -. DR eggNOG; KOG0563; Eukaryota. DR InParanoid; P37830; -. DR SABIO-RK; P37830; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; P37830; baseline. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central. 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 1: Evidence at protein level; KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1..511 FT /note="Glucose-6-phosphate 1-dehydrogenase, cytoplasmic FT isoform" FT /id="PRO_0000068101" FT ACT_SITE 270 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 36..43 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 71 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 151 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 178 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 208..212 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 246 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 265 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 356 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 361 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 392 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" SQ SEQUENCE 511 AA; 58471 MW; BBD9E4891DA62671 CRC64; MAASWCIEKR GSIRNDSFRD NDNIPETGCL SIIVLGASGD LAKKKTFPAL FNLYRQGFLQ SNEVHIFGYA RTKISDDDLR SRIRGYLSQG KENEGEVSEF LQLIKYVSGS YDSAEGFTSL DKAISEHEFS KNSTEGSSRR LFYFALPPSV YPSVCRMIKS YCMNKSDLGG WTRTVVEKPF GKDLASSEQL SSQIGELFDE PQIYRIDHYL GKELVQNLLV LRFANRFFLP LWNRDNIDNI QIVFREDFGT EGRGGYFDEY GIIRDIIQNH LLQVLCLVAM EKPVSQKPEH IRDEKVKVLQ SMLPIEDEEV VLGQYEGYKD DPTVPNNSNT PTFATMVLRI HNERWEGVPF IMKAGKALNS RKAEIRVQFK DVPGDIFRCQ KQGRNEFVIR LQPSEAMYMK LTVKKPGLEM STVQSELDLS YGQRYQGVVI PEAYERLILD TIRGDQQHFV RRDELKAAWE IFTPLLHRID NGEVKPIPYK PGSRGPAEAD ELLQNAGYVQ THGYIWIPPT L //