THIO_MYCTU
ID THIO_MYCTU Reviewed; 116 AA.
AC P9WG67; L0TDX8; P0A616; P52229;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
DE AltName: Full=MPT46;
GN Name=trxA; Synonyms=trx, trxC; OrderedLocusNames=Rv3914;
GN ORFNames=MTV028.05;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wieles B., Phillip W., Drijfhout J.W., Offringa R., Ottenhoff T.H.M.;
RT "Sequence analysis and functional characterization of thioredoxin and
RT thioredoxin reductase of Mycobacterium tuberculosis.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=7591163; DOI=10.1128/iai.63.12.4946-4948.1995;
RA Wieles B., Nagai S., Wiker H.G., Harboe M., Ottenhoff T.H.M.;
RT "Identification and functional characterization of thioredoxin of
RT Mycobacterium tuberculosis.";
RL Infect. Immun. 63:4946-4948(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=17139080; DOI=10.1107/s0907444906038212;
RA Hall G., Shah M., McEwan P.A., Laughton C., Stevens M., Westwell A.,
RA Emsley J.;
RT "Structure of Mycobacterium tuberculosis thioredoxin C.";
RL Acta Crystallogr. D 62:1453-1457(2006).
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; X95798; CAA65071.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46743.1; -; Genomic_DNA.
DR PIR; B70851; B70851.
DR RefSeq; NP_218431.1; NC_000962.3.
DR RefSeq; WP_003400164.1; NZ_NVQJ01000005.1.
DR PDB; 2I1U; X-ray; 1.30 A; A=1-116.
DR PDB; 2L4Q; NMR; -; A=1-116.
DR PDB; 2L59; NMR; -; A=1-116.
DR PDB; 3O6T; X-ray; 2.40 A; A/B/C/D=1-116.
DR PDBsum; 2I1U; -.
DR PDBsum; 2L4Q; -.
DR PDBsum; 2L59; -.
DR PDBsum; 3O6T; -.
DR AlphaFoldDB; P9WG67; -.
DR BMRB; P9WG67; -.
DR SMR; P9WG67; -.
DR STRING; 83332.Rv3914; -.
DR PaxDb; P9WG67; -.
DR DNASU; 886241; -.
DR GeneID; 45427914; -.
DR GeneID; 886241; -.
DR KEGG; mtu:Rv3914; -.
DR TubercuList; Rv3914; -.
DR eggNOG; COG3118; Bacteria.
DR OMA; QVGVAPK; -.
DR PhylomeDB; P9WG67; -.
DR Reactome; R-HSA-1222538; Tolerance by Mtb to nitric oxide produced by macrophages.
DR Reactome; R-HSA-1222541; Cell redox homeostasis.
DR Reactome; R-MTU-936721; Cysteine synthesis from O-acetylserine.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:MTBBASE.
DR GO; GO:0009055; F:electron transfer activity; IDA:MTBBASE.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IDA:MTBBASE.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:MTBBASE.
DR GO; GO:0080007; F:S-nitrosoglutathione reductase activity; IDA:MTBBASE.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7591163"
FT CHAIN 2..116
FT /note="Thioredoxin"
FT /id="PRO_0000120117"
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,
FT ECO:0000269|PubMed:17139080"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:2L59"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2I1U"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2I1U"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:2I1U"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2I1U"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2I1U"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:2I1U"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:2I1U"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2I1U"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2I1U"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:2I1U"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:2I1U"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:2I1U"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:2I1U"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3O6T"
SQ SEQUENCE 116 AA; 12544 MW; 3B7B9AC90B44B571 CRC64;
MTDSEKSATI KVTDASFATD VLSSNKPVLV DFWATWCGPC KMVAPVLEEI ATERATDLTV
AKLDVDTNPE TARNFQVVSI PTLILFKDGQ PVKRIVGAKG KAALLRELSD VVPNLN
