ID   GSHRP_PEA               Reviewed;         552 AA.
AC   P27456;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Glutathione reductase, chloroplastic/mitochondrial;
DE            Short=GR;
DE            Short=GRase;
DE            EC=1.8.1.7;
DE   AltName: Full=GOR1;
DE   Flags: Precursor;
GN   Name=GR; Synonyms=GOR1;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=1303792; DOI=10.1111/j.1365-313x.1992.00129.x;
RA   Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P.M.;
RT   "Molecular characterization of glutathione reductase cDNAs from pea (Pisum
RT   sativum L.).";
RL   Plant J. 2:129-131(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Birte;
RX   PubMed=8904805; DOI=10.1007/bf00208308;
RA   Mullineaux P.M., Enard C., Hellens R., Creissen G.;
RT   "Characterisation of a glutathione reductase gene and its genetic locus
RT   from pea (Pisum sativum L.).";
RL   Planta 200:186-194(1996).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7670502; DOI=10.1046/j.1365-313x.1995.08020167.x;
RA   Creissen G.P., Reynolds H., Xue Y., Mullineaux P.M.;
RT   "Simultaneous targeting of pea glutathione reductase and of a bacterial
RT   fusion protein to chloroplasts and mitochondria in transgenic tobacco.";
RL   Plant J. 8:167-175(1995).
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       {ECO:0000269|PubMed:7670502}. Mitochondrion
CC       {ECO:0000269|PubMed:7670502}. Note=The majority of the protein is found
CC       in chloroplast, with only 3% in mitochondria.
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA42921.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X60373; CAA42921.1; ALT_INIT; mRNA.
DR   EMBL; X90996; CAA62482.1; -; Genomic_DNA.
DR   PIR; S18973; S18973.
DR   AlphaFoldDB; P27456; -.
DR   SMR; P27456; -.
DR   EnsemblPlants; Psat6g057720.1; Psat6g057720.1.cds; Psat6g057720.
DR   Gramene; Psat6g057720.1; Psat6g057720.1.cds; Psat6g057720.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0045454; P:cell redox homeostasis; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP;
KW   Oxidoreductase; Plastid; Redox-active center; Transit peptide.
FT   TRANSIT         1..60
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           61..552
FT                   /note="Glutathione reductase, chloroplastic/mitochondrial"
FT                   /id="PRO_0000030281"
FT   REGION          527..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        515
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         112..121
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..126
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  59108 MW;  690D1058AE4168BC CRC64;
     MNQAMATPLS LSCCSPTLTR STLFFTKTFP FSRSFSTPLP LSTKTLISLS PPHRTFAVRA
     ESQNGADPAR QYDFDLFTIG AGSGGVRASR FASNFGASSA VCELPFSTIS SDTTGGVGGT
     CVIRGCVPKK LLVYASKFSH EFEESNGFGW RYDSEPKHDW SSLIANKNAE LQRLTGIYKN
     TLKNAGVKLI EGRGKIVDAH TVDVDGKLYS AKHILVSVGG RPFIPDIPGK EYAIDSDAAL
     DLPSKPQKIA IVGGGYIALE FAGIFNGLKS EVHVFIRQKK VLRGFDEEIR DFVAENMALR
     GIEFHTEESP VAITKAADGS LSLKTNKGTE EGFSHIMFAT GRSPNTKDLG LESVGVKVAK
     DGSIEVDEYS QTSVPSIWAI GDATNRVNLT PVALMEGVAL AKTLFQNEPT KPDYRAIPSA
     VFSQPPIGGV GLTEEQAAEQ YGDIDVFTAN FRPMKATLSG LPDRVFMKLI VSAETNVVLG
     LHMCGEDAAE IAQGFAVGIK AGLTKADFDA TVGIHPTAAE EFVTMRTPTR KVRKNQASQG
     KSDSKAKAVA GS
//