Y892_MYCTO
ID Y892_MYCTO Reviewed; 495 AA.
AC P9WNG0; L0T532; P64745; Q10532;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Uncharacterized monooxygenase MT0916;
DE EC=1.14.13.-;
GN OrderedLocusNames=MT0916;
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45162.1; -; Genomic_DNA.
DR PIR; A70782; A70782.
DR RefSeq; WP_003404651.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNG0; -.
DR SMR; P9WNG0; -.
DR EnsemblBacteria; AAK45162; AAK45162; MT0916.
DR GeneID; 45424855; -.
DR KEGG; mtc:MT0916; -.
DR PATRIC; fig|83331.31.peg.984; -.
DR HOGENOM; CLU_006937_7_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..495
FT /note="Uncharacterized monooxygenase MT0916"
FT /id="PRO_0000427133"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 286
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 55039 MW; 08CB55F48674DB44 CRC64;
MTGRCPTVAV VGAGMSGMCV AITLLSAGIT DVCIYEKADD VGGTWRDNTY PGLTCDVPSR
LYQYSFAKNP NWTQMFSRGG EIQDYLRGIA ERYGLRHRIR FGATVVSARF DDGRWVLRTD
SGTESTVDFL ISATGVLHHP RIPPIAGLDD FRGTVFHSAR WDHTVPLLGR RIAVIGTGST
GVQLVCGLAG VAGKVTMFQR TAQWVLPWPN PRYSKLARVF HRAFPCLGSL AYKAYSLSFE
TFAVALSNPG LHRKLVGAVC RASLRRVRDP RLRRALTPDY EPMCKRLVMS GGFYRAIQRD
DVELVTAGID HVEHRGIVTD DGVLHEVDVI VLATGFDSHA FFRPMQLTGR DGIRIDDVWQ
DGPHAHQTVA IPGFPNFFMM LGPHSPVGNF PLTAVAESQA EHIVQWIKRW RHGEFDTMEP
KSAATEAYNT VLRAAMPNTV WTTGCDSWYL NKDGIPEVWP FAPAKHRAML ANLHPEEYDL
RRYAAVRATS RPQSA