ID   GLRX1_RICBR             Reviewed;          98 AA.
AC   Q1RHJ0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Glutaredoxin 1;
GN   Name=grxC1; Synonyms=grx; OrderedLocusNames=RBE_1093;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC       presence of NADPH and glutathione reductase. Reduces low molecular
CC       weight disulfides and proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; CP000087; ABE05174.1; -; Genomic_DNA.
DR   RefSeq; WP_011477752.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHJ0; -.
DR   SMR; Q1RHJ0; -.
DR   STRING; 336407.RBE_1093; -.
DR   EnsemblBacteria; ABE05174; ABE05174; RBE_1093.
DR   KEGG; rbe:RBE_1093; -.
DR   eggNOG; COG0695; Bacteria.
DR   HOGENOM; CLU_026126_7_3_5; -.
DR   OMA; GRTTFPQ; -.
DR   OrthoDB; 2045232at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03418; GRX_GRXb_1_3_like; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011900; GRX_bact.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02181; GRX_bact; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..98
FT                   /note="Glutaredoxin 1"
FT                   /id="PRO_0000288734"
FT   DOMAIN          1..98
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        17..20
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   98 AA;  11161 MW;  C8CD5CF1004CA730 CRC64;
     MNKAILHAII IYTLAGCPYC MKAKALLDKK EVAYEEIEVQ NSQDPNVAVL RKKLNNPDRL
     TFPQIFIDNM HIGGCDDLYD LDKEGRLDKL LEGQPKKD