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GLRX4_BUCBP
ID   GLRX4_BUCBP             Reviewed;         108 AA.
AC   Q89AR8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, 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; OrderedLocusNames=bbp_176;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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; AE016826; AAO26908.1; -; Genomic_DNA.
DR   RefSeq; WP_011091309.1; NC_004545.1.
DR   AlphaFoldDB; Q89AR8; -.
DR   SMR; Q89AR8; -.
DR   STRING; 224915.bbp_176; -.
DR   EnsemblBacteria; AAO26908; AAO26908; bbp_176.
DR   GeneID; 56470718; -.
DR   KEGG; bab:bbp_176; -.
DR   eggNOG; COG0278; Bacteria.
DR   HOGENOM; CLU_026126_2_1_6; -.
DR   OMA; KGTKLMP; -.
DR   OrthoDB; 2001991at2; -.
DR   Proteomes; UP000000601; 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..108
FT                   /note="Glutaredoxin 4"
FT                   /id="PRO_0000102256"
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   108 AA;  12065 MW;  B00FDE9D5318F334 CRC64;
     MNDIIKKIQN QIQNNPIIIY MKGSPDAPSC GFSAQAVHAI SSCGKKFAYI DVLKNPDIRL
     ELPKYANWPT FPQLWVNGEL IGGCNIILEL FQKGELKKTI SICDKLNS
 
 
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