ID   MTR_MYCTO               Reviewed;         459 AA.
AC   P9WHH2; L0TB27; O07927; Q6MX25; Q7D6G4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Mycothione reductase;
DE            EC=1.8.1.15;
DE   AltName: Full=Mycothiol-disulfide reductase;
DE   AltName: Full=NADPH-dependent mycothione reductase;
GN   Name=mtr; Synonyms=gorA; OrderedLocusNames=MT2922;
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 [GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RA   Song J., Deretic V.;
RT   "Mycobacterium tuberculosis gorA homolog, complete coding sequence.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of mycothione (the
CC       oxidized disulfide form of mycothiol) to mycothiol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 mycothiol + NADP(+) = H(+) + mycothione + NADPH;
CC         Xref=Rhea:RHEA:12685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16086,
CC         ChEBI:CHEBI:16768, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.15;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 mycothiol + NAD(+) = H(+) + mycothione + NADH;
CC         Xref=Rhea:RHEA:12689, ChEBI:CHEBI:15378, ChEBI:CHEBI:16086,
CC         ChEBI:CHEBI:16768, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.15;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47247.1; -; Genomic_DNA.
DR   PIR; B70590; B70590.
DR   RefSeq; WP_003414557.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHH2; -.
DR   SMR; P9WHH2; -.
DR   EnsemblBacteria; AAK47247; AAK47247; MT2922.
DR   KEGG; mtc:MT2922; -.
DR   PATRIC; fig|83331.31.peg.3155; -.
DR   HOGENOM; CLU_016755_1_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050627; F:mycothione reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR017817; Mycothione_reductase.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR03452; mycothione_red; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..459
FT                   /note="Mycothione reductase"
FT                   /id="PRO_0000428187"
FT   ACT_SITE        444
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         31..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..44
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  49946 MW;  D243DD752E0B043E CRC64;
     METYDIAIIG TGSGNSILDE RYASKRAAIC EQGTFGGTCL NVGCIPTKMF VYAAEVAKTI
     RGASRYGIDA HIDRVRWDDV VSRVFGRIDP IALSGEDYRR CAPNIDVYRT HTRFGPVQAD
     GRYLLRTDAG EEFTAEQVVI AAGSRPVIPP AILASGVDYH TSDTVMRIAE LPEHIVIVGS
     GFIAAEFAHV FSALGVRVTL VIRGSCLLRH CDDTICERFT RIASTKWELR THRNVVDGQQ
     RGSGVALRLD DGCTINADLL LVATGRVSNA DLLDAEQAGV DVEDGRVIVD EYQRTSARGV
     FALGDVSSPY LLKHVANHEA RVVQHNLLCD WEDTQSMIVT DHRYVPAAVF TDPQIAAVGL
     TENQAVAKGL DISVKIQDYG DVAYGWAMED TSGIVKLITE RGSGRLLGAH IMGYQASSLI
     QPLIQAMSFG LTAAEMARGQ YWIHPALPEV VENALLGLR