ID   THIO_MYCPN              Reviewed;         102 AA.
AC   P75512;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; Synonyms=trx; OrderedLocusNames=MPN_263; ORFNames=MP570;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=9202470; DOI=10.1099/00221287-143-6-1933;
RA   Ben-Menachem G., Himmelreich R., Herrmann R., Aharonowitz Y., Rottem S.;
RT   "The thioredoxin reductase system of mycoplasmas.";
RL   Microbiology 143:1933-1940(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; U51987; AAC45450.1; -; Genomic_DNA.
DR   EMBL; U00089; AAB96218.1; -; Genomic_DNA.
DR   PIR; S73896; S73896.
DR   RefSeq; NP_109951.1; NC_000912.1.
DR   RefSeq; WP_010874620.1; NC_000912.1.
DR   AlphaFoldDB; P75512; -.
DR   SMR; P75512; -.
DR   IntAct; P75512; 1.
DR   STRING; 272634.MPN_263; -.
DR   EnsemblBacteria; AAB96218; AAB96218; MPN_263.
DR   GeneID; 66609091; -.
DR   KEGG; mpn:MPN_263; -.
DR   PATRIC; fig|272634.6.peg.282; -.
DR   HOGENOM; CLU_090389_14_0_14; -.
DR   OMA; KIKICKF; -.
DR   BioCyc; MPNE272634:G1GJ3-414-MON; -.
DR   Proteomes; UP000000808; 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   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; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..102
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120114"
FT   DOMAIN          2..102
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        30..33
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   102 AA;  11215 MW;  0D17B97E976FC144 CRC64;
     MVTEIKSLKQ LGELFASNNK VIIDFWAEWC GPCKITGPEF AKAASEVSTV AFAKVNVDEQ
     TDIAAAYKIT SLPTIVLFEK GQEKHRAIGF MPKAKIVQLV SQ