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GLRX4_SHIFL
ID   GLRX4_SHIFL             Reviewed;         115 AA.
AC   P0AC72; P37010; P77424;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Glutaredoxin 4;
DE            Short=Grx4;
DE   AltName: Full=Monothiol glutaredoxin;
GN   Name=grxD; Synonyms=ydhD; OrderedLocusNames=SF1682, S1814;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-
CC       sulfur clusters. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN43261.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17150.1; -; Genomic_DNA.
DR   RefSeq; NP_707554.1; NC_004337.2.
DR   RefSeq; WP_000108172.1; NZ_WPGW01000025.1.
DR   AlphaFoldDB; P0AC72; -.
DR   SMR; P0AC72; -.
DR   STRING; 198214.SF1682; -.
DR   EnsemblBacteria; AAN43261; AAN43261; SF1682.
DR   EnsemblBacteria; AAP17150; AAP17150; S1814.
DR   GeneID; 1024840; -.
DR   GeneID; 67415642; -.
DR   KEGG; sfl:SF1682; -.
DR   KEGG; sfx:S1814; -.
DR   PATRIC; fig|198214.7.peg.1987; -.
DR   HOGENOM; CLU_026126_2_1_6; -.
DR   OMA; KGTKLMP; -.
DR   OrthoDB; 2001991at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03028; GRX_PICOT_like; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR014434; Monothiol_GRX.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR10293; PTHR10293; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PIRSF; PIRSF005894; Monothiol_GRX; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00365; TIGR00365; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Redox-active center;
KW   Reference proteome.
FT   CHAIN           1..115
FT                   /note="Glutaredoxin 4"
FT                   /id="PRO_0000102260"
FT   DOMAIN          5..107
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   BINDING         22
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         84..85
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   115 AA;  12879 MW;  254B540430632645 CRC64;
     MSTTIEKIQR QIAENPILLY MKGSPKLPSC GFSAQAVQAL AACGERFAYV DILQNPDIRA
     ELPKYANWPT FPQLWVDGEL VGGCDIVIEM YQRGELQQLI KETAAKYKSE EPDAE
 
 
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