(data stored in ACNUC9435 zone)

SWISSPROT: THIO_LISIN

ID   THIO_LISIN              Reviewed;         103 AA.
AC   P0A4L4; Q9S386;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=lin1196;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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}.
DR   EMBL; AL596167; CAC96427.1; -; Genomic_DNA.
DR   PIR; AC1582; AC1582.
DR   RefSeq; WP_003723853.1; NC_003212.1.
DR   SMR; P0A4L4; -.
DR   STRING; 272626.lin1196; -.
DR   EnsemblBacteria; CAC96427; CAC96427; CAC96427.
DR   GeneID; 39648313; -.
DR   KEGG; lin:trxA; -.
DR   eggNOG; ENOG4105K63; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000292977; -.
DR   KO; K03671; -.
DR   OMA; DANQEFA; -.
DR   OrthoDB; 1630944at2; -.
DR   BioCyc; GCF_000195795:LIN_RS06100-MONOMER; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
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;
DR   PRODOM; P0A4L4.
DR   SWISS-2DPAGE; P0A4L4.
KW   Disulfide bond; Electron transport; Oxidoreductase; Redox-active center;
KW   Transport.
FT   CHAIN           1..103
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120110"
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
//

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