ID   THIO_ACESD              Reviewed;         105 AA.
AC   P81109; Q9EV95;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; OrderedLocusNames=CLOST_1109;
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=11271425; DOI=10.1007/s002030000232;
RA   Graentzdoerffer A., Pich A., Andreesen J.R.;
RT   "Molecular analysis of the grd-operon encoded proteins of the glycine
RT   reductase and thioredoxin system from Clostridium sticklandii.";
RL   Arch. Microbiol. 175:8-18(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-33.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=9534247; DOI=10.1099/00221287-144-3-793;
RA   Harms C., Meyer M.A., Andreesen J.R.;
RT   "Fast purification of thioredoxin reductases and of thioredoxins with an
RT   unusual redox-active centre from anaerobic, amino-acid-utilizing
RT   bacteria.";
RL   Microbiology 144:793-800(1998).
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.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AJ276209; CAC14298.1; -; Genomic_DNA.
DR   EMBL; FP565809; CBH21231.1; -; Genomic_DNA.
DR   AlphaFoldDB; P81109; -.
DR   SMR; P81109; -.
DR   STRING; 1511.CLOST_1109; -.
DR   EnsemblBacteria; CBH21231; CBH21231; CLOST_1109.
DR   KEGG; cst:CLOST_1109; -.
DR   eggNOG; COG3118; Bacteria.
DR   HOGENOM; CLU_090389_10_2_9; -.
DR   OMA; IQVDVDK; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
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   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Electron transport;
KW   Redox-active center; Reference proteome; Transport.
FT   CHAIN           1..105
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120092"
FT   DOMAIN          1..105
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        29..32
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   105 AA;  11972 MW;  19DA0A9508FE5727 CRC64;
     MFELDKDTFE TEVLQGTGYV LVDFWSEGCE PCKALMPDIQ EMEKTYGEQV RFTKLDTTKA
     RRLAIKEKVL GLPTIAIYKD GQKIDELTKE DATAANVEAM VKKYI