ID A0A1N6MYL4_9GAMM Unreviewed; 113 AA.
AC A0A1N6MYL4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN Name=grxD {ECO:0000313|EMBL:SIP73912.1};
GN ORFNames=XIS1_480038 {ECO:0000313|EMBL:SIP73912.1};
OS Xenorhabdus innexi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=290109 {ECO:0000313|EMBL:SIP73912.1, ECO:0000313|Proteomes:UP000196435};
RN [1] {ECO:0000313|Proteomes:UP000196435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB1681 (deposited as PTA-6826 in the American Type Culture
RC Collection) {ECO:0000313|Proteomes:UP000196435};
RA Gaudriault S.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; FTLG01000190; SIP73912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6MYL4; -.
DR OrthoDB; 9804115at2; -.
DR Proteomes; UP000196435; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000196435}.
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 113 AA; 12902 MW; 4072B4C385A89C9D CRC64;
MTTIEKIERQ IKENPILLYM KGSPKLPSCG FSAQAVQALS ACGERFAYVD ILQNPDIRAE
LPKYANWPTF PQLWVDGELV GGCDILMEMY QRGELQTLIK ETADKYREQE DSQ
//
