ID   GLRX1_SALTI             Reviewed;          87 AA.
AC   P0A1P9; Q9Z5Z3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Glutaredoxin 1;
DE            Short=Grx1;
GN   Name=grxA; OrderedLocusNames=STY0905, t2024;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: The disulfide bond functions as an electron carrier in the
CC       glutathione-dependent synthesis of deoxyribonucleotides by the enzyme
CC       ribonucleotide reductase. In addition, it is also involved in reducing
CC       some disulfides in a coupled system with glutathione reductase (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD05311.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69636.1; -; Genomic_DNA.
DR   RefSeq; NP_455399.1; NC_003198.1.
DR   RefSeq; WP_000495513.1; NZ_WSUR01000019.1.
DR   AlphaFoldDB; P0A1P9; -.
DR   SMR; P0A1P9; -.
DR   STRING; 220341.16502075; -.
DR   EnsemblBacteria; AAO69636; AAO69636; t2024.
DR   KEGG; stt:t2024; -.
DR   KEGG; sty:STY0905; -.
DR   PATRIC; fig|220341.7.peg.914; -.
DR   eggNOG; COG0695; Bacteria.
DR   HOGENOM; CLU_026126_7_3_6; -.
DR   OMA; VGGCTEF; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011902; GRXA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02183; GRXA; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis; Disulfide bond; Electron transport;
KW   Redox-active center; Transport.
FT   CHAIN           1..87
FT                   /note="Glutaredoxin 1"
FT                   /id="PRO_0000141582"
FT   DOMAIN          1..87
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        11..14
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   87 AA;  9924 MW;  9BDE71DE3CFF6B7B CRC64;
     MFTVIFGRPG CPYCVRAKEL AEKLSKERDD FNYRYIDIHA EGITKADLEK TVGKPVETVP
     QIFVDQKHIG GCTDFEAWAK ENLNLFA