ID A0A0C4WU64_9GAMM Unreviewed; 109 AA.
AC A0A0C4WU64;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN ORFNames=Achr_39490 {ECO:0000313|EMBL:AJE23335.1};
OS Azotobacter chroococcum NCIMB 8003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE23335.1, ECO:0000313|Proteomes:UP000068210};
RN [1] {ECO:0000313|EMBL:AJE23335.1, ECO:0000313|Proteomes:UP000068210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE23335.1,
RC ECO:0000313|Proteomes:UP000068210};
RX PubMed=26061173;
RA Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT (ATCC 4412).";
RL PLoS ONE 10:E0127997-E0127997(2015).
CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC {ECO:0000256|ARBA:ARBA00009630, ECO:0000256|PIRNR:PIRNR005894}.
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DR EMBL; CP010415; AJE23335.1; -; Genomic_DNA.
DR RefSeq; WP_039806990.1; NZ_CP010415.1.
DR AlphaFoldDB; A0A0C4WU64; -.
DR STRING; 1328314.Achr_39490; -.
DR KEGG; acx:Achr_39490; -.
DR HOGENOM; CLU_026126_2_1_6; -.
DR Proteomes; UP000068210; 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:UP000068210}.
FT DOMAIN 19..83
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT BINDING 24
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT BINDING 32
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 61
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT BINDING 73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
FT BINDING 86..87
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR005894-1"
SQ SEQUENCE 109 AA; 11824 MW; 2EB0D19D780A8C02 CRC64;
MQTLDTEARI RKQIAENPVI LYMKGTPAAP ECGFSRAAVG ALSKIGKPFA FVNVLAAPHI
REKLPKLFQW PTFPQLFVNG ELIGGCDIIL EMEADGSLQA LLEKATAQA
//
