ID H6PV52_RICP3 Unreviewed; 107 AA.
AC H6PV52;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN OrderedLocusNames=RSA_06355 {ECO:0000313|EMBL:AFB26749.1};
OS Rickettsia philipii (strain 364D).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=481009 {ECO:0000313|EMBL:AFB26749.1, ECO:0000313|Proteomes:UP000007997};
RN [1] {ECO:0000313|Proteomes:UP000007997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=364D {ECO:0000313|Proteomes:UP000007997};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT "Complete genome sequence of Rickettsia philipii strain 364D.";
RL Submitted (FEB-2012) 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; CP003308; AFB26749.1; -; Genomic_DNA.
DR RefSeq; WP_014364987.1; NC_016930.1.
DR AlphaFoldDB; H6PV52; -.
DR KEGG; rph:RSA_06355; -.
DR HOGENOM; CLU_026126_2_1_5; -.
DR OrthoDB; 9804115at2; -.
DR Proteomes; UP000007997; 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 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 107 AA; 12254 MW; 1A1C15ED00DA0B39 CRC64;
MLENKNFKFI ENEIKNNKVV LFMKGIKKSP ACGFSGTVVA ILNKLGVEFR DINVLFDAEL
REDVKKFSDW PTFPQLYING ELVGGCDIAR ELYQSGELEK MLKAYTR
//
