ID   MMAA4_MYCTA             Reviewed;         301 AA.
AC   A5U027; P72028; P96933;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
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;
DE            Short=SAM-MT;
GN   Name=mmaA4; OrderedLocusNames=MRA_0653;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN OXYGEN-CONTAINING
RP   MYCOLATES BIOSYNTHESIS.
RX   PubMed=8917504; DOI=10.1073/pnas.93.23.12828;
RA   Yuan Y., Barry C.E. III;
RT   "A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic
RT   acids in Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12828-12833(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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:8917504}.
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; U66108; AAC44619.1; -; Genomic_DNA.
DR   EMBL; CP000611; ABQ72377.1; -; Genomic_DNA.
DR   PIR; G70613; G70613.
DR   RefSeq; WP_003900195.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U027; -.
DR   SMR; A5U027; -.
DR   STRING; 419947.MRA_0653; -.
DR   EnsemblBacteria; ABQ72377; ABQ72377; MRA_0653.
DR   GeneID; 45424602; -.
DR   KEGG; mra:MRA_0653; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_3_0_11; -.
DR   OMA; YHPYDLA; -.
DR   OrthoDB; 1518440at2; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IMP:UniProtKB.
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..301
FT                   /note="Hydroxymycolate synthase MmaA4"
FT                   /id="PRO_0000398367"
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"
FT   CONFLICT        109
FT                   /note="H -> L (in Ref. 1; AAC44619)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  34670 MW;  827ED04835956802 CRC64;
     MTRMAEKPIS PTKTRTRFED IQAHYDVSDD FFALFQDPTR TYSCAYFEPP ELTLEEAQYA
     KVDLNLDKLD LKPGMTLLDI GCGWGTTMRR AVERFDVNVI GLTLSKNQHA RCEQVLASID
     TNRSRQVLLQ GWEDFAEPVD RIVSIEAFEH FGHENYDDFF KRCFNIMPAD GRMTVQSSVS
     YHPYEMAARG KKLSFETARF IKFIVTEIFP GGRLPSTEMM VEHGEKAGFT VPEPLSLRPH
     YIKTLRIWGD TLQSNKDKAI EVTSEEVYNR YMKYLRGCEH YFTDEMLDCS LVTYLKPGAA
     A