THIO_MYCBO
ID THIO_MYCBO Reviewed; 116 AA.
AC P0A617; A0A1R3Y5V1; P52229; X2BPP7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
DE AltName: Full=MPT46;
GN Name=trxA; Synonyms=trx, trxC; OrderedLocusNames=BQ2027_MB3945;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU02576.1; -; Genomic_DNA.
DR RefSeq; NP_857580.1; NC_002945.3.
DR RefSeq; WP_003400164.1; NC_002945.4.
DR AlphaFoldDB; P0A617; -.
DR BMRB; P0A617; -.
DR SMR; P0A617; -.
DR EnsemblBacteria; SIU02576; SIU02576; BQ2027_MB3945.
DR GeneID; 45427914; -.
DR PATRIC; fig|233413.5.peg.4323; -.
DR OMA; QVGVAPK; -.
DR Proteomes; UP000001419; 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; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..116
FT /note="Thioredoxin"
FT /id="PRO_0000120118"
FT DOMAIN 2..113
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 37..40
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 116 AA; 12544 MW; 3B7B9AC90B44B571 CRC64;
MTDSEKSATI KVTDASFATD VLSSNKPVLV DFWATWCGPC KMVAPVLEEI ATERATDLTV
AKLDVDTNPE TARNFQVVSI PTLILFKDGQ PVKRIVGAKG KAALLRELSD VVPNLN