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Database: UniProt
Entry: A0A0F7LZZ2_9GAMM
LinkDB: A0A0F7LZZ2_9GAMM
Original site: A0A0F7LZZ2_9GAMM 
ID   A0A0F7LZZ2_9GAMM        Unreviewed;       109 AA.
AC   A0A0F7LZZ2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN   ORFNames=IMCC21906_01151 {ECO:0000313|EMBL:AKH68830.1};
OS   Spongiibacter sp. IMCC21906.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Spongiibacter.
OX   NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH68830.1, ECO:0000313|Proteomes:UP000035013};
RN   [1] {ECO:0000313|EMBL:AKH68830.1, ECO:0000313|Proteomes:UP000035013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH68830.1,
RC   ECO:0000313|Proteomes:UP000035013};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21906 belonging to the
RT   Gammaproteobacteria.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC       {ECO:0000256|ARBA:ARBA00009630, ECO:0000256|PIRNR:PIRNR005894}.
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DR   EMBL; CP011477; AKH68830.1; -; Genomic_DNA.
DR   RefSeq; WP_047011348.1; NZ_CP011477.1.
DR   AlphaFoldDB; A0A0F7LZZ2; -.
DR   STRING; 1620392.IMCC21906_01151; -.
DR   KEGG; spoi:IMCC21906_01151; -.
DR   PATRIC; fig|1620392.3.peg.1209; -.
DR   OrthoDB; 9804115at2; -.
DR   Proteomes; UP000035013; 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:UP000035013}.
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   109 AA;  11819 MW;  CA3D20FB6F171B0B CRC64;
     MDTIEAIKQQ IDSNPIILYM KGSPNQPQCG FSAKASQALM GCGERFAFVD ILSNPDIRAK
     LPEVGNWPTF PQLWVAGELV GGCDIICEMH DTGELQTLIK EAVAAQPAQ
//
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