ID B7L5K7_ECO55 Unreviewed; 115 AA.
AC B7L5K7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN Name=ydhD {ECO:0000313|EMBL:CAU97681.1};
GN OrderedLocusNames=EC55989_1822 {ECO:0000313|EMBL:CAU97681.1};
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055 {ECO:0000313|EMBL:CAU97681.1, ECO:0000313|Proteomes:UP000000746};
RN [1] {ECO:0000313|Proteomes:UP000000746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-
CC sulfur clusters. {ECO:0000256|ARBA:ARBA00002853}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000256|ARBA:ARBA00009630, ECO:0000256|PIRNR:PIRNR005894}.
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DR EMBL; CU928145; CAU97681.1; -; Genomic_DNA.
DR RefSeq; WP_000108172.1; NZ_CP028304.1.
DR AlphaFoldDB; B7L5K7; -.
DR SMR; B7L5K7; -.
DR GeneID; 83576732; -.
DR KEGG; eck:EC55989_1822; -.
DR HOGENOM; CLU_026126_2_1_6; -.
DR Proteomes; UP000000746; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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 NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 1.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF72; MONOTHIOL GLUTAREDOXIN-S14, CHLOROPLASTIC; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PIRSF; PIRSF005894; Monothiol_GRX; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR005894-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR005894-2};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR005894-
KW 2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR005894-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000746}.
FT DOMAIN 17..81
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT BINDING 22
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
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:0000256|PIRSR:PIRSR005894-2"
FT BINDING 59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT BINDING 71
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT BINDING 84..85
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
SQ SEQUENCE 115 AA; 12879 MW; 254B540430632645 CRC64;
MSTTIEKIQR QIAENPILLY MKGSPKLPSC GFSAQAVQAL AACGERFAYV DILQNPDIRA
ELPKYANWPT FPQLWVDGEL VGGCDIVIEM YQRGELQQLI KETAAKYKSE EPDAE
//
