ID A0A0G3IFE9_9MYCO Unreviewed; 297 AA.
AC A0A0G3IFE9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:AKK26200.1};
GN ORFNames=AB431_05285 {ECO:0000313|EMBL:AKK26200.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK26200.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK26200.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK26200.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP011773; AKK26200.1; -; Genomic_DNA.
DR RefSeq; WP_047329047.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IFE9; -.
DR STRING; 1545728.AB431_05285; -.
DR KEGG; mye:AB431_05285; -.
DR PATRIC; fig|1545728.4.peg.1076; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000035237; 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 Methyltransferase {ECO:0000313|EMBL:AKK26200.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKK26200.1}.
FT ACT_SITE 274
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
FT BINDING 38..39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 73..81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 99..104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 128..129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
SQ SEQUENCE 297 AA; 33956 MW; C42A381D4D050D66 CRC64;
MPEATETKDM RPHFEDIQAH YDLSDDFFGL FQDPTRKYSC AYFTGPNVTL SEAQIANVDQ
HLDRLDLKPG MTLLEVGCGW GLTLQRAMEK YDVNVIGLTL SKNQKAYCDQ LLAKVDSERT
FDVRLEGWEQ FHSPVDRIVS IEAFEHFGFE RYDDFFKNSF DILPEDGRMT VQSSCGYHPY
DLQARGKKLT FELARFAKFI GEVIFPGGRI PSTQMMVDHG EKAGFTVLEP LSLRNHYIKT
LGIWAARLEQ HKDEAIAAAG EESYNNYMRY LTGCQYYFVD EQLDVSLVTY LKPGAAA
//
