THIO_MYCGE
ID THIO_MYCGE Reviewed; 102 AA.
AC P47370; Q49453;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=trxA; Synonyms=trx; OrderedLocusNames=MG124;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD12321.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L43967; AAC71342.1; -; Genomic_DNA.
DR EMBL; U01796; AAD12321.1; ALT_INIT; Genomic_DNA.
DR PIR; G64213; G64213.
DR RefSeq; WP_010869343.1; NC_000908.2.
DR AlphaFoldDB; P47370; -.
DR SMR; P47370; -.
DR STRING; 243273.MG_124; -.
DR EnsemblBacteria; AAC71342; AAC71342; MG_124.
DR KEGG; mge:MG_124; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_090389_14_0_14; -.
DR OMA; KIKICKF; -.
DR OrthoDB; 1630944at2; -.
DR BioCyc; MGEN243273:G1GJ2-137-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
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; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..102
FT /note="Thioredoxin"
FT /id="PRO_0000120113"
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; 11498 MW; FC08F02C4170EA2D CRC64;
MVTEIRSLKQ LEEIFSAKKN VIVDFWAAWC GPCKLTSPEF QKAADEFSDA QFVKVNVDDH
TDIAAAYNIT SLPTIVVFEN GVEKKRAIGF MPKTKIIDLF NN