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Database: UniProt
Entry: C5BE40_EDWI9
LinkDB: C5BE40_EDWI9
Original site: C5BE40_EDWI9 
ID   C5BE40_EDWI9            Unreviewed;       114 AA.
AC   C5BE40;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN   OrderedLocusNames=NT01EI_2105 {ECO:0000313|EMBL:ACR69281.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR69281.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR69281.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR69281.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT   a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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; CP001600; ACR69281.1; -; Genomic_DNA.
DR   RefSeq; WP_015871412.1; NC_012779.2.
DR   AlphaFoldDB; C5BE40; -.
DR   STRING; 67780.B6E78_03135; -.
DR   GeneID; 69539034; -.
DR   KEGG; eic:NT01EI_2105; -.
DR   PATRIC; fig|634503.3.peg.1882; -.
DR   HOGENOM; CLU_026126_2_1_6; -.
DR   OrthoDB; 9804115at2; -.
DR   Proteomes; UP000001485; 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}.
FT   DOMAIN          16..80
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   BINDING         21
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT   BINDING         29
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         58
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT   BINDING         70
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT   BINDING         83..84
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
SQ   SEQUENCE   114 AA;  12594 MW;  4B8FDF5CB58C0E9F CRC64;
     MTTIEKIQRQ IAENPIILYM KGSPKLPSCG FSAQAVQALS ACGERFAYVD ILQNPDIRAE
     LPKFADWPTF PQLWVEGELI GGCDIILEMY QRGELQTLIK EAAARHGSAA QDNG
//
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