ID   THIO_MYCGA              Reviewed;         100 AA.
AC   Q9R6P9;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=trxA; Synonyms=trx; OrderedLocusNames=MYCGA6330; ORFNames=MGA_0452;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A5969Var.B;
RX   PubMed=11959450; DOI=10.1111/j.1574-6968.2002.tb11095.x;
RA   Skamrov A.V., Feoktistova E.S., Gol'dman M.A., Bibilashvili R.S.;
RT   "Mycoplasma gallisepticum rpoA gene cluster.";
RL   FEMS Microbiol. Lett. 208:281-285(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; L35043; AAF19044.1; -; Genomic_DNA.
DR   EMBL; AE015450; AAP56983.2; -; Genomic_DNA.
DR   RefSeq; WP_011113892.1; NC_004829.2.
DR   AlphaFoldDB; Q9R6P9; -.
DR   SMR; Q9R6P9; -.
DR   KEGG; mga:MGA_0452; -.
DR   PATRIC; fig|233150.7.peg.710; -.
DR   HOGENOM; CLU_090389_14_6_14; -.
DR   OMA; KIKICKF; -.
DR   OrthoDB; 1630944at2; -.
DR   Proteomes; UP000001418; 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..100
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120112"
FT   DOMAIN          1..100
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"
FT   CONFLICT        15
FT                   /note="S -> T (in Ref. 1; AAF19044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="V -> I (in Ref. 1; AAF19044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="R -> I (in Ref. 1; AAF19044)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   100 AA;  11549 MW;  B2A8ADAC82BA3968 CRC64;
     MKHITNKAEL DQLLSTNKKV VVDFYANWCG PCKILGPIFE EVAQDKKDWT FVKVDVDQAN
     EISSEYEIRS IPTVIFFQDG KMADKRIGFI PKNELKELLK