GSHRP_PEA
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 03-AUG-2022, entry version 136.
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).
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 (NADPH) 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; -; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01424; gluta_reduc_2; 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
