ID G6PDC_SPIOL Reviewed; 574 AA. AC O24357; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 08-NOV-2023, entry version 109. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase, chloroplastic; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:Q43727}; DE Flags: Precursor; GN Name=G6PD; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Matador; TISSUE=Leaf; RA Fink A., Diogon T., Perroud P.F., Crespi P., Greppin H.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. 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 provide reducing power (NADPH) and pentose phosphates for fatty acid CC and nucleic acid synthesis which are involved in membrane synthesis and CC cell division. {ECO:0000250|UniProtKB:Q43727}. 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:0000250|UniProtKB:Q43727}; CC -!- ACTIVITY REGULATION: Regulated by metabolites. Post-translationally CC inactivated by cysteine-mediated redox modification via the ferredoxin- CC thioredoxin system in the light and this avoids futile cycles with CC photosynthetic CO2 fixation (By similarity). CC {ECO:0000250|UniProtKB:Q43839}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000305}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11411}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. 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; AJ000182; CAA03939.1; -; mRNA. DR PIR; T09088; T09088. DR AlphaFoldDB; O24357; -. DR SMR; O24357; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP001155700; Unplaced. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-KW. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:UniProt. 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:SF13; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE 1, CHLOROPLASTIC; 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 2: Evidence at transcript level; KW Carbohydrate metabolism; Chloroplast; Disulfide bond; Glucose metabolism; KW NADP; Oxidoreductase; Plastid; Reference proteome; Transit peptide. FT TRANSIT 1..? FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN ?..574 FT /note="Glucose-6-phosphate 1-dehydrogenase, chloroplastic" FT /id="PRO_0000010439" FT ACT_SITE 322 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 93..100 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 127 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 230 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 260..264 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 317 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 418 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 459 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT DISULFID 145..153 FT /note="Redox modulation" FT /evidence="ECO:0000250|UniProtKB:Q43839" SQ SEQUENCE 574 AA; 65180 MW; D498DB32D25849AA CRC64; MEELVSCHHL PLLCLQSSVP PNGCLTFFQD SACQRCSHSE FSNGHPLNDV SLQNDVAVNP IVAKSIDPSA DLQLLPLLES VKEEPTLSII VVGASGDLAK KKIFPALFAL FYENCLPENF TVFGFSRTEM NDEELRTMIS KTLTCRIDQR ENCGEKMDHF LQRCFYHSGQ YNSEDDFSGL DCKLKEKEAG RLQNRLFYLS IPPNIFVDVV RCVSHRASSA SGWTRVIVEK PFGRDSDSSR ELTRSFKQYL SEDQIFRIDH YLGKELVENL SVLRFSNLVF EPLWSRNYIR NVQLIFSEDF GTEGRGGYFD NYGIIRDIMQ NHLLQILALF AMETPVSLDA EDIRNEKVKV LRSMKPLKLQ DVVVGQYKGH SKGNKSYSGY TDDPTVPNNS VTPTFAAAAL FIDNARWDGV PFLMKAGKAL HTKRAEIRVQ FRHVPGNLYK KTFGTDLDKA TNELVLRVQP DEAIYLKINN KVPGLGMRLD RTDLNLCYST RYRGEIPDAY ERLLLDAIEG ERRLFIRSDK LDAAWSLFTP LLKELEEKKV APELYPYGSR GPVGAHYLAA KHNVRWGDLS GEDS //