ID A0A024JT77_9MYCO Unreviewed; 287 AA.
AC A0A024JT77;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Mycolic acid synthase PcaA {ECO:0000313|EMBL:CDO86816.1};
GN Name=pcaA {ECO:0000313|EMBL:CDO86816.1};
GN ORFNames=BN973_01163 {ECO:0000313|EMBL:CDO86816.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO86816.1};
RN [1] {ECO:0000313|EMBL:CDO86816.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86816.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO86816.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86816.1};
RA Xu Y.W., Yang Q.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; HG964446; CDO86816.1; -; Genomic_DNA.
DR RefSeq; WP_036466508.1; NZ_LQPY01000021.1.
DR AlphaFoldDB; A0A024JT77; -.
DR STRING; 47839.BN973_01163; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_3_0_11; -.
DR OrthoDB; 9782855at2; -.
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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT ACT_SITE 269
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
FT BINDING 33..34
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 68..76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 94..99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
SQ SEQUENCE 287 AA; 32817 MW; 8F0900EDD1901063 CRC64;
MAVQLTPQFG NVQAHYDLSD DFFRLFLDPS QTYSCAYFER DDMTLEEAQL AKIDLSLSKL
NLQPGMTLLD IGCGWGATLR RAIEKYDVNV VGLTLSENQA EHVQKSFDQL DSTRTRRVLL
EGWEKFDEPV DRIVSIGAFE HFGRARWARF FEMAYSVLPA DGVMMLHTIV RPAFKEARAK
GLPLTHEVVH FTQFILAEIF PGGWLPTPAL VEEHACDAGF KLTRIQSLQL HYARTLDMWA
AALEANKDNA IEVQSQKVYD RYMKYLTGCA KLFRQGYTDV DQFTLEK
//
