THIO_SALTY
ID THIO_SALTY Reviewed; 109 AA.
AC P0AA28; P00274; P76750; Q47674; Q8XAT2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Thioredoxin 1;
DE Short=Trx-1;
GN Name=trxA; OrderedLocusNames=STM3915; ORFNames=STMD1.75;
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=LT2;
RX PubMed=1561103; DOI=10.1093/nar/20.6.1424;
RA Kotani H., Nakajima K.;
RT "Cloning and sequence of thioredoxin gene of Salmonella typhimurium LT2.";
RL Nucleic Acids Res. 20:1424-1424(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=8253691; DOI=10.1128/jb.175.24.8030-8037.1993;
RA Miloso M., Limauro D., Alifano P., Rivellini F., Lavitola A., Gulletta E.,
RA Bruni C.B.;
RT "Characterization of the rho genes of Neisseria gonorrhoeae and Salmonella
RT typhimurium.";
RL J. Bacteriol. 175:8030-8037(1993).
RN [3]
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: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin 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; D10015; BAA00903.1; -; Genomic_DNA.
DR EMBL; Z21789; CAA79851.1; -; Genomic_DNA.
DR EMBL; AF233324; AAF33471.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22765.1; -; Genomic_DNA.
DR PIR; S35497; S35497.
DR RefSeq; NP_462806.1; NC_003197.2.
DR RefSeq; WP_001280776.1; NC_003197.2.
DR PDB; 1M7T; NMR; -; A=69-108.
DR PDBsum; 1M7T; -.
DR AlphaFoldDB; P0AA28; -.
DR BMRB; P0AA28; -.
DR SMR; P0AA28; -.
DR STRING; 99287.STM3915; -.
DR PaxDb; P0AA28; -.
DR PRIDE; P0AA28; -.
DR EnsemblBacteria; AAL22765; AAL22765; STM3915.
DR GeneID; 1255441; -.
DR GeneID; 64173577; -.
DR GeneID; 67514182; -.
DR KEGG; stm:STM3915; -.
DR PATRIC; fig|99287.12.peg.4137; -.
DR HOGENOM; CLU_090389_10_2_6; -.
DR OMA; QVGVAPK; -.
DR PhylomeDB; P0AA28; -.
DR BioCyc; SENT99287:STM3915-MON; -.
DR PHI-base; PHI:2644; -.
DR PRO; PR:P0AA28; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..109
FT /note="Thioredoxin 1"
FT /id="PRO_0000120100"
FT DOMAIN 2..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 36
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 27
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 34
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 35
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 33..36
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1M7T"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1M7T"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:1M7T"
SQ SEQUENCE 109 AA; 11807 MW; EF5933EA29668EE9 CRC64;
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN
IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLA
