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Database: UniProt
Entry: G6EZD2_9PROT
LinkDB: G6EZD2_9PROT
Original site: G6EZD2_9PROT 
ID   G6EZD2_9PROT            Unreviewed;       109 AA.
AC   G6EZD2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN   ORFNames=CIN_08020 {ECO:0000313|EMBL:EHD14870.1};
OS   Commensalibacter intestini A911.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD14870.1, ECO:0000313|Proteomes:UP000005939};
RN   [1] {ECO:0000313|EMBL:EHD14870.1, ECO:0000313|Proteomes:UP000005939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A911 {ECO:0000313|EMBL:EHD14870.1,
RC   ECO:0000313|Proteomes:UP000005939};
RA   Lee W.-J., Kim E.-K.;
RT   "Genome Sequence of Commensalibacter intestini A911, isolated from
RT   Drosophila gut.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC       {ECO:0000256|ARBA:ARBA00009630, ECO:0000256|PIRNR:PIRNR005894}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHD14870.1}.
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DR   EMBL; AGFR01000003; EHD14870.1; -; Genomic_DNA.
DR   AlphaFoldDB; G6EZD2; -.
DR   STRING; 1088868.CIN_08020; -.
DR   PATRIC; fig|1088868.3.peg.804; -.
DR   eggNOG; COG0278; Bacteria.
DR   OrthoDB; 9804115at2; -.
DR   Proteomes; UP000005939; Unassembled WGS sequence.
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          18..82
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   BINDING         23
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT   BINDING         31
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         60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT   BINDING         72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT   BINDING         85..86
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
SQ   SEQUENCE   109 AA;  12108 MW;  274F4CD45AB4D303 CRC64;
     MSNPVFDQIK NEIDSNDVVL YMKGTADFPS CGFSAKVAHI LSDLGVSFKD INILEDDSLR
     QGLKEFSSWP TFPQLYVKGE LVGGCDIVRE MYASGELAQL LKDKQIACR
//
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