MMAA3_MYCBO
ID MMAA3_MYCBO Reviewed; 293 AA.
AC Q7U1K0; A0A1R3XVY7; P94924; Q9ZH74; X2BFP0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Methoxy mycolic acid synthase MmaA3;
DE EC=2.1.1.-;
DE AltName: Full=Mycolic acid methyltransferase;
DE Short=MA-MT;
DE AltName: Full=S-adenosylmethionine-dependent methyltransferase;
DE Short=AdoMet-MT;
DE Short=SAM-MT;
GN Name=cmaB; Synonyms=mmaA3, mmas-3; OrderedLocusNames=BQ2027_MB0662C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NOMENCLATURE.
RC STRAIN=BCG / Pasteur;
RX PubMed=9044265; DOI=10.1046/j.1365-2958.1997.2301589.x;
RA Dubnau E., Laneelle M.-A., Soares S., Benichou A., Vaz T., Prome D.,
RA Prome J.-C., Daffe M., Quemard A.;
RT "Mycobacterium bovis BCG genes involved in the biosynthesis of cyclopropyl
RT keto- and hydroxy-mycolic acids.";
RL Mol. Microbiol. 23:313-322(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [4]
RP FUNCTION IN OXYGEN-CONTAINING MYCOLATES BIOSYNTHESIS.
RX PubMed=9781881; DOI=10.1046/j.1365-2958.1998.01026.x;
RA Yuan Y., Zhu Y., Crane D.D., Barry C.E. III;
RT "The effect of oxygenated mycolic acid composition on cell wall function
RT and macrophage growth in Mycobacterium tuberculosis.";
RL Mol. Microbiol. 29:1449-1458(1998).
RN [5]
RP FUNCTION IN O-METHYLATED MYCOLIC ACID BIOSYNTHESIS.
RX PubMed=10852869; DOI=10.1128/jb.182.12.3394-3399.2000;
RA Behr M.A., Schroeder B.G., Brinkman J.N., Slayden R.A., Barry C.E. III;
RT "A point mutation in the mma3 gene is responsible for impaired
RT methoxymycolic acid production in Mycobacterium bovis BCG strains obtained
RT after 1927.";
RL J. Bacteriol. 182:3394-3399(2000).
CC -!- FUNCTION: Involved in the biosynthesis of methoxymycolic acid. It
CC catalyzes the O-methylation of the hydroxy group of the hydroxymycolate
CC to form a methyl ether. {ECO:0000269|PubMed:10852869,
CC ECO:0000269|PubMed:9781881}.
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC -!- MISCELLANEOUS: Strain BCG / Pasteur fails to produce methoxymycolic
CC acid due to amino acid alterations in the coding sequence of the mmaA3
CC gene, but is able to produce ketomycolic acid.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; U77466; AAC44875.1; -; Genomic_DNA.
DR EMBL; LT708304; SIT99260.1; -; Genomic_DNA.
DR RefSeq; NP_854320.1; NC_002945.3.
DR RefSeq; WP_003403302.1; NC_002945.4.
DR AlphaFoldDB; Q7U1K0; -.
DR SMR; Q7U1K0; -.
DR EnsemblBacteria; SIT99260; SIT99260; BQ2027_MB0662C.
DR GeneID; 45424603; -.
DR PATRIC; fig|233413.5.peg.722; -.
DR OMA; FHRYDDF; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR003333; Mycolic_cyclopropane_synthase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF003085; CMAS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..293
FT /note="Methoxy mycolic acid synthase MmaA3"
FT /id="PRO_0000398363"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 78..80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 100..105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 129..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="S -> F (in Ref. 1; AAC44875)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="G -> D (in Ref. 1; AAC44875)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..179
FT /note="MLLHSITGLH -> DAAALDHRLAR (in Ref. 1; AAC44875)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> G (in Ref. 1; AAC44875)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="I -> V (in Ref. 1; AAC44875)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="E -> Q (in Ref. 1; AAC44875)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="K -> E (in Ref. 1; AAC44875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 33263 MW; 0897FA680944C63F CRC64;
MSDNSTGTTK SRSNVDDVQA HYDLSDAFFA LFQDPTRTYS CAYFERDDMT LHEAQVAKLD
LTLGKLGLEP GMTLLDVGCG WGSVMKRAVE RYDVNVVGLT LSKNQHAYCQ QVLDKVDTNR
SHRVLLSDWA NFSEPVDRIV TIEAIEHFGF ERYDDFFKFA YNAMPADGVM LLHSITGLHV
KQVIERGIPL TMEMAKFIRF IVTDIFPGGR LPTIETIEEH VTKAGFTITD IQSLQPHFAR
TLDLWAEALQ AHKDEAIEIQ SAEVYERYMK YLTGCAKAFR MGYIDCNQFT LAK
