GSHRP_SOYBN
ID GSHRP_SOYBN Reviewed; 544 AA.
AC P48640;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glutathione reductase, chloroplastic;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
DE Flags: Precursor;
GN Name=GR;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root nodule;
RX PubMed=8165247; DOI=10.1104/pp.104.3.1081;
RA Tang X., Webb M.A.;
RT "Soybean root nodule cDNA encoding glutathione reductase.";
RL Plant Physiol. 104:1081-1082(1994).
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 {ECO:0000305}.
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; L11632; AAA33962.1; -; mRNA.
DR PIR; T07155; T07155.
DR RefSeq; NP_001238006.1; NM_001251077.1.
DR AlphaFoldDB; P48640; -.
DR SMR; P48640; -.
DR STRING; 3847.GLYMA02G16010.3; -.
DR PRIDE; P48640; -.
DR GeneID; 547793; -.
DR KEGG; gmx:547793; -.
DR eggNOG; KOG0405; Eukaryota.
DR InParanoid; P48640; -.
DR OrthoDB; 581771at2759; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0009507; C:chloroplast; 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:0004791; F:thioredoxin-disulfide reductase 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; -; 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; NADP; Oxidoreductase;
KW Plastid; Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..544
FT /note="Glutathione reductase, chloroplastic"
FT /id="PRO_0000030282"
FT REGION 519..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 507
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 105..113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 113..118
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 544 AA; 58783 MW; 7A71449EA21CE639 CRC64;
MATSLSVSPS LSLNTLFIAK ALPLSRPSFL SLPLPKSLLS LSTRRRTFIV RAESQNGRDP
VPAHYDFDLF TIGAGSGGVR ARRFAANYGA SVAICELPFS TISSETTGVG GTCVIRGCVP
KKLLVYASKF SHEFEESNGF GWRYDSEPKH DWSSFIANKN AELQRLTGIY KNILNNAGVK
LIEGHGKMID PHTVDVNGKL YSAKHILVAV GGRPFIPDIP GKELAIDSDA ALDLPTKPVK
IAIVGGGYIA LEFAGIFNGL KSEVHVFIRQ KKVLRGFDEE IRDFVEEQMS VRGIEFHTEE
SPQAITKSAD GSFSLKTNKG TVDGFSHIMF ATGRRPNTQN LGLESVGVKL AKDGAIEVDE
YSQTSVYSIW AVGDVTNRIN LTPVALMEGG ALVKTLFQDN PTKPDYRAVP SAVFSQPPIG
QVGLTEEQAV QQYGDIDIFT ANFRPLKATL SGLPDRVFMK LVVCAKTNEV LGLHMCGEDA
PEIVQGFAVA LKARLTKADF DATVGIHPSA AEEFVTMRTP TRKIRKSESS EGKSGSQAKA
AAGV
