ID   MYMA_MYCTU              Reviewed;         495 AA.
AC   P9WNF7; F2GNY5; L0TBT0; O53300; Q7D658;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Putative FAD-containing monooxygenase MymA;
DE            EC=1.14.13.-;
GN   Name=mymA; OrderedLocusNames=Rv3083;
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   INDUCTION, AND GENE NAME.
RX   PubMed=14568148; DOI=10.1016/s0378-1097(03)00648-7;
RA   Singh A., Jain S., Gupta S., Das T., Tyagi A.K.;
RT   "mymA operon of Mycobacterium tuberculosis: its regulation and importance
RT   in the cell envelope.";
RL   FEMS Microbiol. Lett. 227:53-63(2003).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Erdman;
RX   PubMed=15937179; DOI=10.1128/jb.187.12.4173-4186.2005;
RA   Singh A., Gupta R., Vishwakarma R.A., Narayanan P.R., Paramasivan C.N.,
RA   Ramanathan V.D., Tyagi A.K.;
RT   "Requirement of the mymA operon for appropriate cell wall ultrastructure
RT   and persistence of Mycobacterium tuberculosis in the spleens of guinea
RT   pigs.";
RL   J. Bacteriol. 187:4173-4186(2005).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16893682; DOI=10.1016/j.tube.2006.01.021;
RA   Cheruvu M., Plikaytis B.B., Shinnick T.M.;
RT   "The acid-induced operon Rv3083-Rv3089 is required for growth of
RT   Mycobacterium tuberculosis in macrophages.";
RL   Tuberculosis 87:12-20(2007).
RN   [5]
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: Required for maintaining the appropriate mycolic acid
CC       composition and permeability of the envelope on its exposure to acidic
CC       pH. {ECO:0000269|PubMed:15937179}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- INDUCTION: Expression is controlled by VirS. Induced at acidic pH and
CC       in macrophages. {ECO:0000269|PubMed:14568148}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the mymA operon causes altered
CC       cell wall structure, reduced contents and altered composition of
CC       mycolic acids along with the accumulation of saturated C24 and C26
CC       fatty acids, and enhanced susceptibility to antibiotics, detergents and
CC       acidic pH. Also impairs ability to survive in macrophages.
CC       {ECO:0000269|PubMed:15937179, ECO:0000269|PubMed:16893682}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45892.1; -; Genomic_DNA.
DR   PIR; G70852; G70852.
DR   RefSeq; NP_217599.1; NC_000962.3.
DR   RefSeq; WP_003899906.1; NZ_NVQJ01000011.1.
DR   AlphaFoldDB; P9WNF7; -.
DR   SMR; P9WNF7; -.
DR   STRING; 83332.Rv3083; -.
DR   BindingDB; P9WNF7; -.
DR   PaxDb; P9WNF7; -.
DR   GeneID; 888655; -.
DR   KEGG; mtu:Rv3083; -.
DR   TubercuList; Rv3083; -.
DR   eggNOG; COG2072; Bacteria.
DR   OMA; ICQEMGW; -.
DR   PhylomeDB; P9WNF7; -.
DR   BioCyc; MetaCyc:G185E-7345-MON; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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   GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR   GO; GO:0010447; P:response to acidic pH; IEP:MTBBASE.
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   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..495
FT                   /note="Putative FAD-containing monooxygenase MymA"
FT                   /id="PRO_0000420876"
FT   BINDING         15
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..57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   SITE            296
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  55482 MW;  756BD62677334926 CRC64;
     MNQHFDVLII GAGLSGIGTA CHVTAEFPDK TIALLERRER LGGTWDLFRY PGVRSDSDMF
     TFGYKFRPWR DVKVLADGAS IRQYIADTAT EFGVDEKIHY GLKVNTAEWS SRQCRWTVAG
     VHEATGETRT YTCDYLISCT GYYNYDAGYL PDFPGVHRFG GRCVHPQHWP EDLDYSGKKV
     VVIGSGATAV TLVPAMAGSN PGSAAHVTML QRSPSYIFSL PAVDKISEVL GRFLPDRWVY
     EFGRRRNIAI QRKLYQACRR WPKLMRRLLL WEVRRRLGRS VDMSNFTPNY LPWDERLCAV
     PNGDLFKTLA SGAASVVTDQ IETFTEKGIL CKSGREIEAD IIVTATGLNI QMLGGMRLIV
     DGAEYQLPEK MTYKGVLLEN APNLAWIIGY TNASWTLKSD IAGAYLCRLL RHMADNGYTV
     ATPRDAQDCA LDVGMFDQLN SGYVKRGQDI MPRQGSKHPW RVLMHYEKDA KILLEDPIDD
     GVLHFAAAAQ DHAAA