ID   GLRX1_RICCN             Reviewed;         102 AA.
AC   Q92J02;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Glutaredoxin 1;
GN   Name=grxC1; Synonyms=grx; OrderedLocusNames=RC0267;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02805.1; -; Genomic_DNA.
DR   PIR; C97733; C97733.
DR   RefSeq; WP_010976927.1; NC_003103.1.
DR   AlphaFoldDB; Q92J02; -.
DR   SMR; Q92J02; -.
DR   EnsemblBacteria; AAL02805; AAL02805; RC0267.
DR   GeneID; 57451984; -.
DR   KEGG; rco:RC0267; -.
DR   HOGENOM; CLU_026126_7_3_5; -.
DR   OMA; GRTTFPQ; -.
DR   Proteomes; UP000000816; 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..102
FT                   /note="Glutaredoxin 1"
FT                   /id="PRO_0000288735"
FT   DOMAIN          1..96
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        17..20
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   102 AA;  11331 MW;  7B7844F027B2C989 CRC64;
     MNKAILHTII VYTLASCPYC IKAKALLDEK NVAYEEIEVS NFTQEEKEKF IKKSGGKKTV
     PQIFIDNMHV GGCDALFDLE KEGRLDKLLE NQPKTTSPAA GA