TRXB_MYCTO
ID TRXB_MYCTO Reviewed; 335 AA.
AC P9WHH0; L0TFM3; O53592; P52214;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Thioredoxin reductase;
DE Short=TR;
DE Short=TRXR;
DE EC=1.8.1.9 {ECO:0000250|UniProtKB:P9WHH1};
GN Name=trxB {ECO:0000303|PubMed:12218036}; Synonyms=trxB2;
GN OrderedLocusNames=MT4032;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P9WHH1};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WHH1};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WHH1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250|UniProtKB:P9WHH1}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK48397.1; -; Genomic_DNA.
DR PIR; A70851; A70851.
DR RefSeq; WP_003900782.1; NZ_KK341228.1.
DR AlphaFoldDB; P9WHH0; -.
DR SMR; P9WHH0; -.
DR EnsemblBacteria; AAK48397; AAK48397; MT4032.
DR GeneID; 45427913; -.
DR KEGG; mtc:MT4032; -.
DR PATRIC; fig|83331.31.peg.4338; -.
DR HOGENOM; CLU_031864_5_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center.
FT CHAIN 1..335
FT /note="Thioredoxin reductase"
FT /id="PRO_0000428188"
FT BINDING 22..25
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 44..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 268
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 295..298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT BINDING 295
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
FT DISULFID 145..148
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P9WHH1"
SQ SEQUENCE 335 AA; 35643 MW; 3D0DD581E6C187E2 CRC64;
MTAPPVHDRA HHPVRDVIVI GSGPAGYTAA LYAARAQLAP LVFEGTSFGG ALMTTTDVEN
YPGFRNGITG PELMDEMREQ ALRFGADLRM EDVESVSLHG PLKSVVTADG QTHRARAVIL
AMGAAARYLQ VPGEQELLGR GVSSCATCDG FFFRDQDIAV IGGGDSAMEE ATFLTRFARS
VTLVHRRDEF RASKIMLDRA RNNDKIRFLT NHTVVAVDGD TTVTGLRVRD TNTGAETTLP
VTGVFVAIGH EPRSGLVREA IDVDPDGYVL VQGRTTSTSL PGVFAAGDLV DRTYRQAVTA
AGSGCAAAID AERWLAEHAA TGEADSTDAL IGAQR
