GSHRC_ARATH
ID GSHRC_ARATH Reviewed; 499 AA.
AC P48641; Q2V3T0; Q94BM6; Q9C5I4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Glutathione reductase, cytosolic;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
DE AltName: Full=OBP29;
GN OrderedLocusNames=At3g24170; ORFNames=MUJ8.7;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Loebler M.;
RT "An Arabidopsis cDNA homologous to glutathione reductase.";
RL (er) Plant Gene Register PGR96-053(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
CC -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
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 {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; U37697; AAB67841.1; -; mRNA.
DR EMBL; AB028621; BAB01358.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76865.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76866.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76867.1; -; Genomic_DNA.
DR EMBL; AF360228; AAK25938.1; -; mRNA.
DR EMBL; AY040029; AAK64087.1; -; mRNA.
DR EMBL; AY140042; AAM98183.1; -; mRNA.
DR EMBL; AY142628; AAN13086.1; -; mRNA.
DR EMBL; BT008870; AAP68309.1; -; mRNA.
DR RefSeq; NP_001030756.2; NM_001035679.2.
DR RefSeq; NP_001118688.1; NM_001125216.1.
DR RefSeq; NP_189059.1; NM_113322.5.
DR AlphaFoldDB; P48641; -.
DR SMR; P48641; -.
DR BioGRID; 7335; 11.
DR DIP; DIP-60756N; -.
DR STRING; 3702.AT3G24170.1; -.
DR MetOSite; P48641; -.
DR PaxDb; P48641; -.
DR PRIDE; P48641; -.
DR ProteomicsDB; 247184; -.
DR EnsemblPlants; AT3G24170.1; AT3G24170.1; AT3G24170.
DR EnsemblPlants; AT3G24170.2; AT3G24170.2; AT3G24170.
DR EnsemblPlants; AT3G24170.3; AT3G24170.3; AT3G24170.
DR GeneID; 822003; -.
DR Gramene; AT3G24170.1; AT3G24170.1; AT3G24170.
DR Gramene; AT3G24170.2; AT3G24170.2; AT3G24170.
DR Gramene; AT3G24170.3; AT3G24170.3; AT3G24170.
DR KEGG; ath:AT3G24170; -.
DR Araport; AT3G24170; -.
DR TAIR; locus:2093691; AT3G24170.
DR eggNOG; KOG0405; Eukaryota.
DR HOGENOM; CLU_016755_2_3_1; -.
DR InParanoid; P48641; -.
DR OMA; CFDYVKP; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; P48641; -.
DR BioCyc; ARA:AT3G24170-MON; -.
DR PRO; PR:P48641; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P48641; baseline and differential.
DR Genevisible; P48641; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IDA:TAIR.
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 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..499
FT /note="Glutathione reductase, cytosolic"
FT /id="PRO_0000067961"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 64..73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 73..78
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 162
FT /note="T -> A (in Ref. 4; AAK25938/AAK64087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 53871 MW; D6B29E8B5B867186 CRC64;
MARKMLVDGE IDKVAADEAN ATHYDFDLFV IGAGSGGVRA ARFSANHGAK VGICELPFHP
ISSEEIGGVG GTCVIRGCVP KKILVYGATY GGELEDAKNY GWEINEKVDF TWKKLLQKKT
DEILRLNNIY KRLLANAAVK LYEGEGRVVG PNEVEVRQID GTKISYTAKH ILIATGSRAQ
KPNIPGHELA ITSDEALSLE EFPKRAIVLG GGYIAVEFAS IWRGMGATVD LFFRKELPLR
GFDDEMRALV ARNLEGRGVN LHPQTSLTQL TKTDQGIKVI SSHGEEFVAD VVLFATGRSP
NTKRLNLEAV GVELDQAGAV KVDEYSRTNI PSIWAVGDAT NRINLTPVAL MEATCFANTA
FGGKPTKAEY SNVACAVFCI PPLAVVGLSE EEAVEQATGD ILVFTSGFNP MKNTISGRQE
KTLMKLIVDE KSDKVIGASM CGPDAAEIMQ GIAIALKCGA TKAQFDSTVG IHPSSAEEFV
TMRSVTRRIA HKPKPKTNL
