ID GSHRP_TOBAC Reviewed; 557 AA. AC P80461; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 08-NOV-2023, entry version 134. DE RecName: Full=Glutathione reductase, chloroplastic; DE Short=GR; DE Short=GRase; DE EC=1.8.1.7; DE Flags: Precursor; Fragment; GN Name=GOR; 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]. RX PubMed=8547821; DOI=10.1007/bf00202667; RA Creissen G.P., Mullineaux P.M.; RT "Cloning and characterisation of glutathione reductase cDNAs and RT identification of two genes encoding the tobacco enzyme."; RL Planta 197:422-425(1995). RN [2] RP PROTEIN SEQUENCE OF 67-74. RC TISSUE=Leaf; RA Willows R.D., Kannangara G.C., Svendsen I.; RL Submitted (JUN-1995) to UniProtKB. CC -!- FUNCTION: Maintains high levels of reduced glutathione in the CC chloroplast. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) + CC NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. {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; X76293; CAA53925.1; -; mRNA. DR PIR; S38908; S38908. DR AlphaFoldDB; P80461; -. DR SMR; P80461; -. DR STRING; 4097.P80461; -. DR PaxDb; 4097-P80461; -. DR BRENDA; 1.8.1.7; 3645. DR Proteomes; UP000084051; Unplaced. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central. DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central. DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf. DR InterPro; IPR006324; GSHR. DR InterPro; IPR046952; GSHR/TRXR-like. DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR NCBIfam; TIGR01424; gluta_reduc_2; 1. DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1. DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW Chloroplast; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; KW NADP; Oxidoreductase; Plastid; Redox-active center; Reference proteome; KW Transit peptide. FT TRANSIT <1..66 FT /note="Chloroplast" FT /evidence="ECO:0000269|Ref.2" FT CHAIN 67..557 FT /note="Glutathione reductase, chloroplastic" FT /id="PRO_0000030284" FT REGION 535..557 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 521 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 118..127 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 283 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 289 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT DISULFID 127..132 FT /note="Redox-active" FT /evidence="ECO:0000250" FT NON_TER 1 SQ SEQUENCE 557 AA; 60035 MW; 79813D1C6AA1D784 CRC64; ATSLSTPKLS TTLSSPTLHS LLYKHKFSLL SLSNPIKPLH FNFLTHSRST PSSLSCTRRR FTAPRAESSN GADAPRHYDF DLFTIGAGSG GVRASRFASN FGASVAVCEL PFSTISSDST GGVGGTCVLR GCVPKKLLVY ASKYSHEFEE SCGFGWNYDV EPRFDWSTLI ANKNAELQRL TGIYKNILKN AGVTLIEGRG KVVDPHTVDV DGKLYSAKNI LISVGGRPFI PDIPGSEYAI DSDAALDLPT KPNKIAIVGG GYIALEFAGI FNGLKSEVHV FIRQKKVLRG FDEEIRDFVG EQMSLRGIEF HTEESPQAIV KSADGSLSLK TSRGTVEGFS HIMFATGRRP NTKNLGLETV GVKMTKNGAI EVDEYSRTSV PSIWAVGDVT DRINLTPVAL MEGGALAKTI FAHEPTKPDY RNVPAAVFSQ PPIGQVGLME EQAIKEFGDV DVYTANFRPL KATISGLPDR VFMKLIVCAK TSKVLGLHMC GDDAPEIVQG FAIAVKAGLT KADFDATVGI HPTSAEEFVT MRTPTRKVRS SPSEGKAEHD IKAAAGV //