GSHRP_ARATH
ID GSHRP_ARATH Reviewed; 565 AA.
AC P42770;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Glutathione reductase, chloroplastic;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2360;
DE Flags: Precursor;
GN Name=EMB2360; OrderedLocusNames=At3g54660; ORFNames=T5N23_20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Columbia;
RA Kubo A., Sano T., Saji H., Tanaka K., Kondo N., Tanaka K.;
RT "Primary structure and properties of glutathione reductase from Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 34:1259-1266(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Columbia;
RA Kubo A.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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}.
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DR EMBL; D14049; BAA03137.1; -; mRNA.
DR EMBL; D89620; BAA19653.1; -; Genomic_DNA.
DR EMBL; AL138650; CAB77586.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79262.1; -; Genomic_DNA.
DR PIR; T47625; T47625.
DR RefSeq; NP_191026.1; NM_115323.4.
DR AlphaFoldDB; P42770; -.
DR SMR; P42770; -.
DR BioGRID; 9947; 16.
DR IntAct; P42770; 1.
DR STRING; 3702.AT3G54660.1; -.
DR SwissPalm; P42770; -.
DR PaxDb; P42770; -.
DR PRIDE; P42770; -.
DR ProteomicsDB; 247185; -.
DR EnsemblPlants; AT3G54660.1; AT3G54660.1; AT3G54660.
DR GeneID; 824631; -.
DR Gramene; AT3G54660.1; AT3G54660.1; AT3G54660.
DR KEGG; ath:AT3G54660; -.
DR Araport; AT3G54660; -.
DR TAIR; locus:2102410; AT3G54660.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_3_1; -.
DR InParanoid; P42770; -.
DR OMA; MSKHYDY; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; P42770; -.
DR BRENDA; 1.8.1.7; 399.
DR PRO; PR:P42770; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P42770; baseline and differential.
DR Genevisible; P42770; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
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..74
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 75..565
FT /note="Glutathione reductase, chloroplastic"
FT /id="PRO_0000030280"
FT REGION 544..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 529
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 126..135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 135..140
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 565 AA; 60852 MW; 29C2CD0E68ED4E4A CRC64;
MASTPKLTST ISSSSPSLQF LCKKLPIAIH LPSSSSSSFL SLPKTLTSLY SLRPRIALLS
NHRYYHSRRF SVCASTDNGA ESDRHYDFDL FTIGAGSGGV RASRFATSFG ASAAVCELPF
STISSDTAGG VGGTCVLRGC VPKKLLVYAS KYSHEFEDSH GFGWKYETEP SHDWTTLIAN
KNAELQRLTG IYKNILSKAN VKLIEGRGKV IDPHTVDVDG KIYTTRNILI AVGGRPFIPD
IPGKEFAIDS DAALDLPSKP KKIAIVGGGY IALEFAGIFN GLNCEVHVFI RQKKVLRGFD
EDVRDFVGEQ MSLRGIEFHT EESPEAIIKA GDGSFSLKTS KGTVEGFSHV MFATGRKPNT
KNLGLENVGV KMAKNGAIEV DEYSQTSVPS IWAVGDVTDR INLTPVALME GGALAKTLFQ
NEPTKPDYRA VPCAVFSQPP IGTVGLTEEQ AIEQYGDVDV YTSNFRPLKA TLSGLPDRVF
MKLIVCANTN KVLGVHMCGE DSPEIIQGFG VAVKAGLTKA DFDATVGVHP TAAEEFVTMR
APTRKFRKDS SEGKASPEAK TAAGV
