GLRX1_SALTY
ID GLRX1_SALTY Reviewed; 87 AA.
AC P0A1P8; Q9Z5Z3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glutaredoxin 1;
DE Short=Grx1;
GN Name=grxA; OrderedLocusNames=STM0872;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29629 / TA 1535;
RA Lambert I.B., Boroumandi S., Nokhbeh M.R., Pokorny N.S., Koziarz P.;
RT "Cloning and characterization of the major nitrotreductase from Salmonella
RT typhimurium TA1535.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF117952; AAD18026.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19808.1; -; Genomic_DNA.
DR RefSeq; NP_459849.1; NC_003197.2.
DR RefSeq; WP_000495513.1; NC_003197.2.
DR AlphaFoldDB; P0A1P8; -.
DR SMR; P0A1P8; -.
DR STRING; 99287.STM0872; -.
DR PaxDb; P0A1P8; -.
DR EnsemblBacteria; AAL19808; AAL19808; STM0872.
DR GeneID; 1252391; -.
DR KEGG; stm:STM0872; -.
DR PATRIC; fig|99287.12.peg.911; -.
DR HOGENOM; CLU_026126_7_3_6; -.
DR OMA; VGGCTEF; -.
DR PhylomeDB; P0A1P8; -.
DR BioCyc; SENT99287:STM0872-MON; -.
DR Proteomes; UP000001014; 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; Reference proteome; Transport.
FT CHAIN 1..87
FT /note="Glutaredoxin 1"
FT /id="PRO_0000141583"
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"
FT CONFLICT 50..53
FT /note="KTVG -> QNRS (in Ref. 1; AAD18026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 87 AA; 9924 MW; 9BDE71DE3CFF6B7B CRC64;
MFTVIFGRPG CPYCVRAKEL AEKLSKERDD FNYRYIDIHA EGITKADLEK TVGKPVETVP
QIFVDQKHIG GCTDFEAWAK ENLNLFA
