ID A0A2X4UCM5_9NOCA Unreviewed; 297 AA.
AC A0A2X4UCM5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cyclopropane fatty acid synthase {ECO:0000313|EMBL:SQI32162.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:SQI32162.1};
GN Name=cmaA1 {ECO:0000313|EMBL:SQI32162.1};
GN ORFNames=NCTC10994_02110 {ECO:0000313|EMBL:SQI32162.1};
OS Rhodococcus coprophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI32162.1, ECO:0000313|Proteomes:UP000249091};
RN [1] {ECO:0000313|EMBL:SQI32162.1, ECO:0000313|Proteomes:UP000249091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI32162.1,
RC ECO:0000313|Proteomes:UP000249091};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; LS483468; SQI32162.1; -; Genomic_DNA.
DR RefSeq; WP_072702742.1; NZ_LS483468.1.
DR AlphaFoldDB; A0A2X4UCM5; -.
DR STRING; 1219011.GCA_001895045_03203; -.
DR KEGG; rcr:NCTC10994_02110; -.
DR Proteomes; UP000249091; Chromosome 1.
DR GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
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:SQI32162.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249091};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SQI32162.1}.
FT ACT_SITE 269
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
FT BINDING 32..33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 67..75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 93..98
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 297 AA; 34692 MW; B076974B342AC3B4 CRC64;
MTKLTPFYEN VQSHYDLSDE FFDLFLDSTR TYSCAYFERD DMSLEEAQKA KIDLSLRKCD
LRPGMTLLDI GCGWGSTMRR AIERYDVNVI GLTLSRNQYD HVSEMISGLA LGRRSAEVRL
QGWEDFDQPV DRIVSIGAFE HFRRRRYDTF FERTSQMLPP DGRMLLHTIV GHSRQLLEDM
QVEVNRDDAL FLRFILREIF PGGQLPERDM IITGAQRHGF WVQNIESLQP HYAHTLDLWA
RALESRHDEA VALASEEVFQ RYMRYLTGCA ENFRRGLIDL QQFTLVKHPR SGAPRTV
//
