GLRX4_ECOL6
ID GLRX4_ECOL6 Reviewed; 115 AA.
AC P0AC70; P37010; P77424;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glutaredoxin 4;
DE Short=Grx4;
DE AltName: Full=Monothiol glutaredoxin;
GN Name=grxD; Synonyms=ydhD; OrderedLocusNames=c2048;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN80508.1; -; Genomic_DNA.
DR RefSeq; WP_000108172.1; NC_004431.1.
DR AlphaFoldDB; P0AC70; -.
DR SMR; P0AC70; -.
DR STRING; 199310.c2048; -.
DR EnsemblBacteria; AAN80508; AAN80508; c2048.
DR GeneID; 67415642; -.
DR KEGG; ecc:c2048; -.
DR eggNOG; COG0278; Bacteria.
DR HOGENOM; CLU_026126_2_1_6; -.
DR OMA; KGTKLMP; -.
DR BioCyc; ECOL199310:C2048-MON; -.
DR Proteomes; UP000001410; 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.
FT CHAIN 1..115
FT /note="Glutaredoxin 4"
FT /id="PRO_0000102259"
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
