MTR_MYCTU
ID MTR_MYCTU Reviewed; 459 AA.
AC P9WHH3; 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 55.
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=Rv2855;
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 [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 [2]
RP PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=10512639; DOI=10.1021/bi991025h;
RA Patel M.P., Blanchard J.S.;
RT "Expression, purification, and characterization of Mycobacterium
RT tuberculosis mycothione reductase.";
RL Biochemistry 38:11827-11833(1999).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS, AND REACTION MECHANISM.
RX PubMed=11318633; DOI=10.1021/bi0029144;
RA Patel M.P., Blanchard J.S.;
RT "Mycobacterium tuberculosis mycothione reductase: pH dependence of the
RT kinetic parameters and kinetic isotope effects.";
RL Biochemistry 40:5119-5126(2001).
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).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of mycothione (the
CC oxidized disulfide form of mycothiol) to mycothiol.
CC {ECO:0000269|PubMed:10512639}.
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 Evidence={ECO:0000269|PubMed:10512639};
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 Evidence={ECO:0000269|PubMed:10512639};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10512639};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10512639};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.7 uM for NADPH {ECO:0000269|PubMed:10512639,
CC ECO:0000269|PubMed:11318633};
CC KM=43 uM for NADH {ECO:0000269|PubMed:10512639,
CC ECO:0000269|PubMed:11318633};
CC KM=70 uM for mycothione {ECO:0000269|PubMed:10512639,
CC ECO:0000269|PubMed:11318633};
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:10512639,
CC ECO:0000269|PubMed:11318633};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10512639}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF002193; AAB63369.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45656.1; -; Genomic_DNA.
DR PIR; B70590; B70590.
DR RefSeq; WP_003414557.1; NZ_NVQJ01000006.1.
DR RefSeq; YP_177910.1; NC_000962.3.
DR AlphaFoldDB; P9WHH3; -.
DR SMR; P9WHH3; -.
DR STRING; 83332.Rv2855; -.
DR ChEMBL; CHEMBL1075170; -.
DR PaxDb; P9WHH3; -.
DR DNASU; 887773; -.
DR GeneID; 887773; -.
DR KEGG; mtu:Rv2855; -.
DR TubercuList; Rv2855; -.
DR eggNOG; COG1249; Bacteria.
DR OMA; MSKHYDY; -.
DR PhylomeDB; P9WHH3; -.
DR BioCyc; MetaCyc:G185E-7106-MON; -.
DR BRENDA; 1.8.1.15; 3445.
DR Reactome; R-MTU-870331; Mycothiol metabolism.
DR SABIO-RK; P9WHH3; -.
DR PRO; PR:P9WHH3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:MTBBASE.
DR GO; GO:0050627; F:mycothione reductase activity; IDA:MTBBASE.
DR GO; GO:0070402; F:NADPH binding; IDA:MTBBASE.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0010126; P:mycothiol metabolic process; TAS:Reactome.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; NAD; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..459
FT /note="Mycothione reductase"
FT /id="PRO_0000399830"
FT ACT_SITE 444
FT /note="Proton acceptor"
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"
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
