ID Q9CBK3_MYCLE Unreviewed; 298 AA.
AC Q9CBK3;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Methyl mycolic acid synthase 4 {ECO:0000313|EMBL:CAC30857.1};
GN Name=mmaA4 {ECO:0000313|EMBL:CAC30857.1};
GN OrderedLocusNames=ML1903 {ECO:0000313|EMBL:CAC30857.1};
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC30857.1, ECO:0000313|Proteomes:UP000000806};
RN [1] {ECO:0000313|EMBL:CAC30857.1, ECO:0000313|Proteomes:UP000000806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN {ECO:0000313|EMBL:CAC30857.1,
RC ECO:0000313|Proteomes:UP000000806};
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; AL583923; CAC30857.1; -; Genomic_DNA.
DR PIR; A87147; A87147.
DR RefSeq; NP_302280.1; NC_002677.1.
DR RefSeq; WP_010908601.1; NC_002677.1.
DR AlphaFoldDB; Q9CBK3; -.
DR KEGG; mle:ML1903; -.
DR PATRIC; fig|272631.5.peg.3606; -.
DR Leproma; ML1903; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_3_0_11; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000000806; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003333; CMAS.
DR InterPro; IPR047672; CMAS_actinobact.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; NF040660; mycolic_MTase; 1.
DR PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR PANTHER; PTHR43667:SF1; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR Pfam; PF02353; CMAS; 1.
DR PIRSF; PIRSF003085; CMAS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000000806};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
FT BINDING 39..40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 74..82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 100..105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 129..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
SQ SEQUENCE 298 AA; 34203 MW; 077CE4C3CE924043 CRC64;
MTEQPTGPTK TRTRSEDIQA HYDLSNEFFA LFQDPTRTYS CAYFEPPDLT LEEAQYAKID
LNLNKLDLKP GMTLLDIGCG WGTTMRRAVE KYDVKVIGLT LSKNQHARCE QVLTALESNR
SRQVRLQGWE DFTEPVDRIV SIEAFEHFGH ENYDDFFKRC FNIMPSDGRM TVQSSVSYHP
FDMAARGKKL SFETARFIKF IITEIFPGGR LPSTKMMVEH GEKAGFTVSE PLSLQSHYVK
TLRIWGDTLE SNRAKAIEVT SEAVYNRYMK YLRGCAHYFS DEMLDCSLVT YLKPGALD
//
