ID   MMAA4_MYCBO             Reviewed;         301 AA.
AC   Q7U1K1; A0A1R3XVY3; P94925; X2BFR1;
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=Hydroxymycolate synthase MmaA4;
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;
GN   Name=cmaA; Synonyms=mmaA4, mmas-4; OrderedLocusNames=BQ2027_MB0661C;
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], FUNCTION IN OXYGEN-CONTAINING MYCOLATES
RP   BIOSYNTHESIS, 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).
CC   -!- FUNCTION: Involved in the biosynthesis of hydroxymycolate, a common
CC       precursor of oxygenated mycolic acids (methoxymycolate and
CC       ketomycolate). Probably transfers a methyl group from the S-
CC       adenosylmethionine (SAM) cofactor and, subsequently or simultaneously,
CC       a water molecule onto the double bound of ethylene substrates, leading
CC       to the formation of the hydroxylated product at the distal position.
CC       {ECO:0000269|PubMed:9044265}.
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC44876.1; Type=Erroneous initiation; Note=Truncated 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; U77466; AAC44876.1; ALT_INIT; Genomic_DNA.
DR   EMBL; LT708304; SIT99259.1; -; Genomic_DNA.
DR   RefSeq; NP_854319.1; NC_002945.3.
DR   RefSeq; WP_003910170.1; NC_002945.4.
DR   AlphaFoldDB; Q7U1K1; -.
DR   SMR; Q7U1K1; -.
DR   EnsemblBacteria; SIT99259; SIT99259; BQ2027_MB0661C.
DR   PATRIC; fig|233413.5.peg.721; -.
DR   OMA; YHPYDLA; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0071768; P:mycolic acid biosynthetic process; IMP:UniProtKB.
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..301
FT                   /note="Hydroxymycolate synthase MmaA4"
FT                   /id="PRO_0000398366"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000250"
FT   BINDING         42..43
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         103..108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         132..133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  34636 MW;  32D9BD2292F800A5 CRC64;
     MTRMAEKPIS PTKTRTRFED IQAHYDVSDD FFALFQDPTR TYSCAYFEPP ELTLEEAQYA
     KVDLNLDKLD LKPGMTLLDI GCGWGTTMRR AVERLDVNVI GLTLSKNQHA RCEQVLASID
     TNRSRQVLLQ GWEDFAEPVD RIVSIEAFEH FGHENYDDFF KRCFNIMPAD GRMTVQSSVS
     YHPYEMAARG KKLSFETARF IKFIVTEIFP GGRLPSTEMM VEHGEKAGFT VPEPLSLRPH
     YIKTLRIWGD TLQSNKDKAI EVTSEEVYNR YMKYLRGCEH YFTDEMLDCS LVTYLKPGAA
     A