ID   GLRX1_RICTY             Reviewed;         104 AA.
AC   Q68XG4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Glutaredoxin 1;
GN   Name=grxC1; Synonyms=grx; OrderedLocusNames=RT0194;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03678.1; -; Genomic_DNA.
DR   RefSeq; WP_011190665.1; NC_006142.1.
DR   AlphaFoldDB; Q68XG4; -.
DR   SMR; Q68XG4; -.
DR   KEGG; rty:RT0194; -.
DR   eggNOG; COG0695; Bacteria.
DR   HOGENOM; CLU_026126_7_3_5; -.
DR   OrthoDB; 9814618at2; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03418; GRX_GRXb_1_3_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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   NCBIfam; TIGR02181; GRX_bact; 1.
DR   PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR   PANTHER; PTHR45694:SF18; GLUTAREDOXIN-1; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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..104
FT                   /note="Glutaredoxin 1"
FT                   /id="PRO_0000288737"
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   104 AA;  11662 MW;  493A295658C5E9BB CRC64;
     MNKSILHTII IYTLASCPYC IKAKALLDKK NVIYEEIEVS NFTQEEKEAF IKKSGGKNTV
     PQIFIDNMHV GGCDDLFNLE QDGRLDKLLE TQPKNKNSLT VSGA
//