MMAA1_MYCTO
ID MMAA1_MYCTO Reviewed; 286 AA.
AC P9WPB0; L0T754; P0A5Q0; P0C5C3; P72025; P94922; P96934;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Mycolic acid methyltransferase MmaA1;
DE EC=2.1.1.-;
DE AltName: Full=S-adenosylmethionine-dependent methyltransferase;
DE Short=AdoMet-MT;
DE Short=SAM-MT;
GN Name=mmaA1; Synonyms=mma1; OrderedLocusNames=MT0673;
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 -!- FUNCTION: Involved in the conversion of a cis-olefin into a trans-
CC olefin with concomitant introduction of an allylic methyl branch at the
CC proximal position of the precursor to both the methoxy and ketomycolic
CC acids. It directly affects the cis- to trans ratio and indirectly
CC affects the keto to methoxy ratio (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK44899.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK44899.1; ALT_INIT; Genomic_DNA.
DR PIR; B70614; B70614.
DR RefSeq; WP_003403310.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPB0; -.
DR SMR; P9WPB0; -.
DR EnsemblBacteria; AAK44899; AAK44899; MT0673.
DR GeneID; 45424605; -.
DR KEGG; mtc:MT0673; -.
DR PATRIC; fig|83331.31.peg.716; -.
DR HOGENOM; CLU_026434_3_0_11; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
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 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..286
FT /note="Mycolic acid methyltransferase MmaA1"
FT /id="PRO_0000426983"
FT ACT_SITE 268
FT /evidence="ECO:0000250"
FT BINDING 32..33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 71..73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 93..98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 122..123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 33149 MW; 229EB252DCA8C552 CRC64;
MAKLRPYYEE SQSAYDISDD FFALFLDPTW VYTCAYFERD DMTLEEAQLA KVDLALDKLN
LEPGMTLLDV GCGWGGALVR AVEKYDVNVI GLTLSRNHYE RSKDRLAAIG TQRRAEARLQ
GWEEFEENVD RIVSFEAFDA FKKERYLTFF ERSYDILPDD GRMLLHSLFT YDRRWLHEQG
IALTMSDLRF LKFLRESIFP GGELPSEPDI VDNAQAAGFT IEHVQLLQQH YARTLDAWAA
NLQAARERAI AVQSEEVYNN FMHYLTGCAE RFRRGLINVA QFTMTK