GSTUN_ARATH
ID GSTUN_ARATH Reviewed; 220 AA.
AC Q9M9F1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glutathione S-transferase U23;
DE Short=AtGSTU23;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 23;
GN Name=GSTU23; OrderedLocusNames=At1g78320; ORFNames=F3F9.14;
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;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12090627; DOI=10.1023/a:1015557300450;
RA Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT family.";
RL Plant Mol. Biol. 49:515-532(2002).
CC -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC a wide number of exogenous and endogenous hydrophobic electrophiles and
CC have a detoxification role against certain herbicides. {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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DR EMBL; AC013430; AAF71800.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36095.1; -; Genomic_DNA.
DR EMBL; BT025286; ABF19039.1; -; mRNA.
DR EMBL; AY085813; AAM63029.1; -; mRNA.
DR PIR; C96812; C96812.
DR RefSeq; NP_177955.1; NM_106481.4.
DR PDB; 5O84; X-ray; 1.88 A; A=3-218.
DR PDB; 6EP6; X-ray; 1.59 A; A/B=1-220.
DR PDB; 6EP7; X-ray; 1.95 A; A/B=1-220.
DR PDBsum; 5O84; -.
DR PDBsum; 6EP6; -.
DR PDBsum; 6EP7; -.
DR AlphaFoldDB; Q9M9F1; -.
DR SMR; Q9M9F1; -.
DR STRING; 3702.AT1G78320.1; -.
DR MetOSite; Q9M9F1; -.
DR PaxDb; Q9M9F1; -.
DR PRIDE; Q9M9F1; -.
DR ProteomicsDB; 247344; -.
DR EnsemblPlants; AT1G78320.1; AT1G78320.1; AT1G78320.
DR GeneID; 844167; -.
DR Gramene; AT1G78320.1; AT1G78320.1; AT1G78320.
DR KEGG; ath:AT1G78320; -.
DR Araport; AT1G78320; -.
DR TAIR; locus:2032035; AT1G78320.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_2_1; -.
DR InParanoid; Q9M9F1; -.
DR OMA; AKMEFME; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9M9F1; -.
DR BioCyc; ARA:AT1G78320-MON; -.
DR PRO; PR:Q9M9F1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9F1; baseline and differential.
DR Genevisible; Q9M9F1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03185; GST_C_Tau; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260; PTHR11260; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Detoxification; Reference proteome; Transferase.
FT CHAIN 1..220
FT /note="Glutathione S-transferase U23"
FT /id="PRO_0000413568"
FT DOMAIN 3..82
FT /note="GST N-terminal"
FT DOMAIN 88..208
FT /note="GST C-terminal"
FT BINDING 13..14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:6EP6"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:6EP6"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6EP6"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6EP6"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:6EP6"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 118..139
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:6EP6"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:6EP6"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:6EP6"
SQ SEQUENCE 220 AA; 25681 MW; B8DCB7497574456E CRC64;
MEEEIILLDY WASMYGMRTR IALEEKKVKY EYREEDLSNK SPLLLQMNPI HKKIPVLIHE
GKPICESIIQ VQYIDELWPD TNPILPSDPY QRAQARFWAD YIDKKTYVPC KALWSESGEK
QEAAKIEFIE VLKTLDSELG DKYYFGGNEF GLVDIAFIGF YSWFRTYEEV ANLSIVLEFP
KLMAWAQRCL KRESVAKALP DSDKVLKSVS DHRKIILGID
