位置:首页 > 蛋白库 > GSTA5_DICDI
GSTA5_DICDI
ID   GSTA5_DICDI             Reviewed;         198 AA.
AC   Q54QV7;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative glutathione S-transferase alpha-5;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha 5;
GN   Name=gsta5; ORFNames=DDB_G0283575;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. {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   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {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; AAFI02000055; EAL65665.1; -; Genomic_DNA.
DR   RefSeq; XP_639027.1; XM_633935.1.
DR   AlphaFoldDB; Q54QV7; -.
DR   SMR; Q54QV7; -.
DR   STRING; 44689.DDB0231408; -.
DR   PaxDb; Q54QV7; -.
DR   EnsemblProtists; EAL65665; EAL65665; DDB_G0283575.
DR   GeneID; 8624155; -.
DR   KEGG; ddi:DDB_G0283575; -.
DR   dictyBase; DDB_G0283575; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   HOGENOM; CLU_039475_1_0_1; -.
DR   InParanoid; Q54QV7; -.
DR   OMA; RVLRMYY; -.
DR   PhylomeDB; Q54QV7; -.
DR   Reactome; R-DDI-156590; Glutathione conjugation.
DR   Reactome; R-DDI-189483; Heme degradation.
DR   Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-9748787; Azathioprine ADME.
DR   Reactome; R-DDI-9753281; Paracetamol ADME.
DR   PRO; PR:Q54QV7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 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   Reference proteome; Transferase.
FT   CHAIN           1..198
FT                   /note="Putative glutathione S-transferase alpha-5"
FT                   /id="PRO_0000350742"
FT   DOMAIN          2..78
FT                   /note="GST N-terminal"
FT   DOMAIN          80..198
FT                   /note="GST C-terminal"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08263"
FT   BINDING         49..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         62..63
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
SQ   SEQUENCE   198 AA;  23298 MW;  A5B154C82270C654 CRC64;
     MTKPTLTYFP VRGRVQFPRC LLEYLGEEYN FNEVKTISDD LRKQLLFKQL PLYQEGDFKI
     VQTPAIIDYI SEKHDFRGKT KEERARAHQC LAGIMEVLDH CLGYSFKMDK QQQEKFRNES
     PIKKFFEGFE MVLSQNKYLA SGEKETYVDL MAFVMVDYVT NLGLMPSGDY PKLISLKKHY
     ESSPQLKKYL ESRPQSNF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024