DHAR4_ARATH
ID DHAR4_ARATH Reviewed; 217 AA.
AC Q9FG59;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable glutathione S-transferase DHAR4;
DE EC=2.5.1.18 {ECO:0000305};
DE AltName: Full=Chloride intracellular channel homolog 4;
DE Short=CLIC homolog 4;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase 4 {ECO:0000305};
DE Short=AtDHAR4 {ECO:0000305};
DE Short=GSH-dependent dehydroascorbate reductase 4;
DE EC=1.8.5.1 {ECO:0000305};
GN Name=DHAR4; OrderedLocusNames=At5g36270; ORFNames=T30G6.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP GENE FAMILY.
RX PubMed=12077129; DOI=10.1074/jbc.m202919200;
RA Dixon D.P., Davis B.G., Edwards R.;
RT "Functional divergence in the glutathione transferase superfamily in
RT plants. Identification of two classes with putative functions in redox
RT homeostasis in Arabidopsis thaliana.";
RL J. Biol. Chem. 277:30859-30869(2002).
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase and
CC dehydroascorbate (DHA) reductase activities.
CC {ECO:0000250|UniProtKB:Q9FWR4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9FWR4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. DHAR family. {ECO:0000305}.
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DR EMBL; AB026661; BAB09367.1; -; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9FG59; -.
DR SMR; Q9FG59; -.
DR PeptideAtlas; Q9FG59; -.
DR PRIDE; Q9FG59; -.
DR Araport; AT5G36270; -.
DR InParanoid; Q9FG59; -.
DR PRO; PR:Q9FG59; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG59; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033355; P:ascorbate glutathione cycle; IEA:InterPro.
DR GO; GO:0010731; P:protein glutathionylation; IBA:GO_Central.
DR InterPro; IPR044627; DHAR1/2/3/4.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44420; PTHR44420; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Detoxification; Oxidoreductase; Reference proteome; Transferase.
FT CHAIN 1..217
FT /note="Probable glutathione S-transferase DHAR4"
FT /id="PRO_0000395484"
FT DOMAIN 10..85
FT /note="GST N-terminal"
FT DOMAIN 86..217
FT /note="GST C-terminal"
FT MOTIF 20..25
FT /note="Glutathione-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 8
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 19
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 19
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 47
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 75
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9FWR4"
FT BINDING 164
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 211
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 214
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
SQ SEQUENCE 217 AA; 24060 MW; FA21044464FDB0EA CRC64;
MGIEVCVKAA SGAPDVLGDC PFGQRILLTL EDKKLPYKTH LIDVSLKPDW FLAISPKGKL
PLVKFDEDEN WVADSDLIVG IIEEKYPEPS LVTFPPEFAS VGSKIIGAFV MFLTSKDHAN
DGSDMALLDE LEALDHHLKT HVGPFVAGDK VTVVDLSLAP KLYHLETTLG HFMDWCVPES
LTNVRDYMKV LFSLESFEKT KAAKEYLIAS WAPKLDV
