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GSTF5_ARATH
ID   GSTF5_ARATH             Reviewed;         256 AA.
AC   Q9SRY6; F4HZ88;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Glutathione S-transferase F5;
DE            Short=AtGSTF5;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-phi member 5;
GN   Name=GSTF5; OrderedLocusNames=At1g02940; ORFNames=F22D16.6;
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   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. Phi family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF02872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009525; AAF02872.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27499.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59676.1; -; Genomic_DNA.
DR   PIR; H86159; H86159.
DR   RefSeq; NP_001322017.1; NM_001331367.1.
DR   RefSeq; NP_001322019.1; NM_001331365.1.
DR   RefSeq; NP_171793.1; NM_100175.2.
DR   AlphaFoldDB; Q9SRY6; -.
DR   SMR; Q9SRY6; -.
DR   STRING; 3702.AT1G02940.1; -.
DR   PaxDb; Q9SRY6; -.
DR   PRIDE; Q9SRY6; -.
DR   ProteomicsDB; 248517; -.
DR   EnsemblPlants; AT1G02940.1; AT1G02940.1; AT1G02940.
DR   EnsemblPlants; AT1G02940.4; AT1G02940.4; AT1G02940.
DR   GeneID; 839479; -.
DR   Gramene; AT1G02940.1; AT1G02940.1; AT1G02940.
DR   Gramene; AT1G02940.4; AT1G02940.4; AT1G02940.
DR   KEGG; ath:AT1G02940; -.
DR   Araport; AT1G02940; -.
DR   TAIR; locus:2024775; AT1G02940.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_5_1_1; -.
DR   InParanoid; Q9SRY6; -.
DR   OrthoDB; 1231780at2759; -.
DR   PRO; PR:Q9SRY6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SRY6; baseline and differential.
DR   Genevisible; Q9SRY6; 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:0043295; F:glutathione binding; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03187; GST_C_Phi; 1.
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; IPR004046; GST_C.
DR   InterPro; IPR034347; GST_Phi_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 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; Reference proteome; Transferase.
FT   CHAIN           1..256
FT                   /note="Glutathione S-transferase F5"
FT                   /id="PRO_0000413543"
FT   DOMAIN          37..118
FT                   /note="GST N-terminal"
FT   DOMAIN          126..256
FT                   /note="GST C-terminal"
FT   BINDING         47..48
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..77
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         89..90
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..103
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   256 AA;  29849 MW;  CF93E7D6D804C46F CRC64;
     MGINASHVPE TCYHHCNQTF ESSRQCFKWC QELARKDEYK IYGYPYSTNT RRVLAVLHEK
     GLSYDPITVN LIAGDQKKPS FLAINPFGQV PVFLDGGLKL TESRAISEYI ATVHKSRGTQ
     LLNYKSYKTM GTQRMWMAIE SFEFDPLTST LTWEQSIKPM YGLKTDYKVV NETEAKLEKV
     LDIYEERLKN SSFLASNSFT MADLYHLPNI QYLMDTHTKR MFVNRPSVRR WVAEITARPA
     WKRACDVKAW YHKKKN
 
 
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