THIO_LISMO
ID THIO_LISMO Reviewed; 103 AA.
AC P0A4L3; Q9S386;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; OrderedLocusNames=lmo1233;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Serovar 1/2a;
RA Tarchanov M., Borovok I., Aharonowitz Y., Cohen G.;
RT "Isolation, cloning and characterization of the Listeria monocytogenes
RT thioredoxin gene, trxA.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase system.
CC Participates in various redox reactions through the reversible
CC oxidation of its active center dithiol to a disulfide and catalyzes
CC dithiol-disulfide exchange reactions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AJ133006; CAB40815.2; -; Genomic_DNA.
DR EMBL; AL591978; CAC99311.1; -; Genomic_DNA.
DR PIR; AI1228; AI1228.
DR RefSeq; NP_464758.1; NC_003210.1.
DR RefSeq; WP_003723853.1; NZ_CP023861.1.
DR AlphaFoldDB; P0A4L3; -.
DR SMR; P0A4L3; -.
DR STRING; 169963.lmo1233; -.
DR PaxDb; P0A4L3; -.
DR EnsemblBacteria; CAC99311; CAC99311; CAC99311.
DR GeneID; 61170220; -.
DR GeneID; 986032; -.
DR KEGG; lmo:lmo1233; -.
DR PATRIC; fig|169963.11.peg.1264; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_4_9; -.
DR OMA; QVGVAPK; -.
DR PhylomeDB; P0A4L3; -.
DR BioCyc; LMON169963:LMO1233-MON; -.
DR PHI-base; PHI:7258; -.
DR Proteomes; UP000000817; 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 3: Inferred from homology;
KW Disulfide bond; Electron transport; Oxidoreductase; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..103
FT /note="Thioredoxin"
FT /id="PRO_0000120111"
FT DOMAIN 1..103
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 28..31
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 103 AA; 11620 MW; 01F6A77434559A46 CRC64;
MVKEITDATF EQETSEGLVL TDFWATWCGP CRMVAPVLEE IQEERGEALK IVKMDVDENP
ETPGSFGVMS IPTLLIKKDG EVVETIIGYR PKEELDEVIN KYV