ID G6PDC_TOBAC Reviewed; 593 AA. AC Q43793; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 08-NOV-2023, entry version 118. 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; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Samsun; TISSUE=Leaf; RA Knight J.S., Emes M.J.; RT "Isolation of a tobacco chloroplast glucose-6-phosphate dehydrogenase RT cDNA."; RL (er) Plant Gene Register PGR96-076(1996). 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 (By similarity). {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. 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; X99405; CAA67782.1; -; mRNA. DR PIR; T03244; T03244. DR RefSeq; NP_001313142.1; NM_001326213.1. DR AlphaFoldDB; Q43793; -. DR SMR; Q43793; -. DR STRING; 4097.Q43793; -. DR PaxDb; 4097-Q43793; -. DR GeneID; 107828938; -. DR KEGG; nta:107828938; -. DR OrthoDB; 312822at2759; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000084051; 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; 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:SF11; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE 2, 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 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 ?..593 FT /note="Glucose-6-phosphate 1-dehydrogenase, chloroplastic" FT /id="PRO_0000010441" FT ACT_SITE 345 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 116..123 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 150 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 253 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 253 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 283..287 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 340 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 441 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 446 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 482 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT DISULFID 168..176 FT /note="Redox modulation" FT /evidence="ECO:0000250|UniProtKB:Q43839" SQ SEQUENCE 593 AA; 67369 MW; 228A7732E510E571 CRC64; MVTLYSSPST HSSGPVASYS NSSIGLYNYH HNKQIAVSSI LSRKFGSLQI NQKPFWNAVR MQDGAVATPP SKIENETPLK KLKNGILPVA PPKEQKDTID FDSNKAKSTV SITVVGASGD LAKKKIFPAL FALYYEGCLP EHFTIFGYAR SKMTDAELRN MVSKTLTCRI DKRENCGEKM EQFLERCFYH SGQYDSLENF AELDKKLKEH EAGRFSNRLF YLSIPPNIFI NAVRCASLSA SSAHGWTRVI VEKPFGRDSE SSAALTRSLK QYLNEDQIFR IDHYLGKELV ENLSVLRFSN LIFEPLWSRQ CIRNVQFIFS EDFGTEGRGG YFDHYGIIRD IMQNHLLQIL ALFAMETPVS LDAEDIRNEK VKVLRSMRPL QLDDVIIGQY KCHTKGDVTY PGYTDDKTVP KDSLTPTFAA AALFIDNARW DGVPFLMKAG KALHTRSAEI RVQFRHVPGN LYNKNFGSDL DQATNELVIR VQPNEAIYLK INNKVPGLGM RLDRSNLNLL YSARYSKEIP DAYERLLLDA IEGERRLFIR SDELDAAWSL FTPVLKELED KKIVPEYYPY GSRGPIGAHY LAARYKVRWG DLV //