GSHRC_PEA
ID GSHRC_PEA Reviewed; 498 AA.
AC Q43621;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glutathione reductase, cytosolic;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
DE AltName: Full=GOR2;
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 STRAIN=cv. Birte; TISSUE=Leaf;
RX PubMed=9349285; DOI=10.1023/a:1005858120232;
RA Stevens R.G., Greissen G.P., Mullineaux P.M.;
RT "Cloning and characterisation of a cytosolic glutathione reductase cDNA
RT from pea (Pisum sativum L.) and its expression in response to stress.";
RL Plant Mol. Biol. 35:641-654(1997).
CC -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC May play a role in the restoration of the post-stress redox state of
CC the cytosolic glutathione pool.
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: Cytoplasm.
CC -!- INDUCTION: Increased expression in the recovery (post-stress) phases of
CC both drought and chilling.
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}.
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DR EMBL; X98274; CAA66924.1; -; mRNA.
DR PIR; T06442; T06442.
DR AlphaFoldDB; Q43621; -.
DR SMR; Q43621; -.
DR EnsemblPlants; Psat1g098440.1; Psat1g098440.1.cds; Psat1g098440.
DR EnsemblPlants; Psat1g098440.2; Psat1g098440.2.cds; Psat1g098440.
DR Gramene; Psat1g098440.1; Psat1g098440.1.cds; Psat1g098440.
DR Gramene; Psat1g098440.2; Psat1g098440.2.cds; Psat1g098440.
DR GO; GO:0005737; C:cytoplasm; 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 Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center.
FT CHAIN 1..498
FT /note="Glutathione reductase, cytosolic"
FT /id="PRO_0000067964"
FT ACT_SITE 471
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 63..72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 72..77
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 498 AA; 53897 MW; 19AD08959764C6D0 CRC64;
MARKMLNDGE PDLKKGEEQG KVYDFDLFII GAGSGGVRAA RFSSNFGAKV GICELPFHPI
SSETIGGVGG TCVIRGCVPK KILVYGASYG GELQDARNFG WELNENVDFN WKKLLQKKTD
EINRLNGIYK RLLSNAGVKL FEGEGKIASP NEVEVTQLDG TKLSYSAKHI LIATGSRAQR
PNIPGQELGI TSDEALSLEE FPKRAVILGG GYIAVEFASI WRGMGSSVNL VFRKELPLRG
FDDEMRAVVA RNLEGRGINL HPRTNLAQLI KTEDGIKVIT DHGEELIADV VLFATGRSPN
SKRLNLEKVG VEFDKAGAIV VDEYSRTNIP SIWAVGDVTN RLNLTPVALM EASLFAKTVF
GGQASKPDYN DIPYAVFCIP PLSVVGLSEE QAVEQTKGDV LIFTSTFNPM KNTISGRQEK
TVMKLVVDAQ TDKVLGASMC GPDAPEIVQG IAIAIKCGAT KAQFDSTVGI HPSSAEEFVT
MRSETRRVTG GVKPKTNL
