MMAA3_MYCTU
ID MMAA3_MYCTU Reviewed; 293 AA.
AC P0CH91; L0T4G3; O08053; P72027; Q79FX7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=mmaA3; Synonyms=mma3; OrderedLocusNames=Rv0643c;
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 FUNCTION IN OXYGEN-CONTAINING MYCOLATES BIOSYNTHESIS.
RC STRAIN=ATCC 25618 / H37Rv;
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 [3]
RP FUNCTION IN O-METHYLATED MYCOLIC ACID BIOSYNTHESIS, AND MUTAGENESIS OF
RP GLY-98.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [4]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
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: 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 -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43386.1; -; Genomic_DNA.
DR PIR; H70613; H70613.
DR RefSeq; NP_215157.1; NC_000962.3.
DR RefSeq; WP_003403302.1; NZ_NVQJ01000007.1.
DR AlphaFoldDB; P0CH91; -.
DR SMR; P0CH91; -.
DR STRING; 83332.Rv0643c; -.
DR PaxDb; P0CH91; -.
DR GeneID; 45424603; -.
DR GeneID; 888058; -.
DR KEGG; mtu:Rv0643c; -.
DR TubercuList; Rv0643c; -.
DR eggNOG; COG2230; Bacteria.
DR InParanoid; P0CH91; -.
DR OMA; FHRYDDF; -.
DR PhylomeDB; P0CH91; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008171; F:O-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0071768; P:mycolic acid biosynthetic process; IDA:MTBBASE.
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 Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..293
FT /note="Methoxy mycolic acid synthase MmaA3"
FT /id="PRO_0000398362"
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 MUTAGEN 98
FT /note="G->D: Loss of O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10852869"
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
