ID A0A0N1NMG7_9ACTN Unreviewed; 436 AA.
AC A0A0N1NMG7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:KPI17083.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:KPI17083.1};
GN ORFNames=OK074_8269 {ECO:0000313|EMBL:KPI17083.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI17083.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI17083.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI17083.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI17083.1}.
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DR EMBL; LJCV01000086; KPI17083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NMG7; -.
DR PATRIC; fig|1592327.3.peg.2775; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
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; IPR020803; PKS_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 SMART; SM00828; PKS_MT; 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:KPI17083.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPI17083.1}.
FT DOMAIN 156..400
FT /note="Polyketide synthase methyltransferase"
FT /evidence="ECO:0000259|SMART:SM00828"
SQ SEQUENCE 436 AA; 48207 MW; 15F609B3F361E7DF CRC64;
MADAASRLQG LVERLLGVPL PVRVRAWDGS EAGPPDAPAL LVRNRRALRR LLWKPGELGL
ARAWVAGDLG IEGDLYAALD LISGLVWERG EDARTLRQAL ADPDVRAAVR GLVKMAGPFP
PPPPPPEEVR RARGHLHTKR SDRRAISHHY DVGNSFYEIV LGPSMVYSCA YWEAPEADGG
TLEDAQRDKL DLVCRKLNLR PGQRLLDVGC GWGSMAVHAA REYGVSVVGV TLSQEQAAYA
RKRVAEEGLT DKVEIRVQDY RDVSDGPYDA ISSIGMAEHV GGERYLEYAR SLHALLAPGG
RLLNHQIARR PQRDESAYSI DEFIDAYVFP DGELAPIGTT VTLLERAGFE VRDVEALREH
YALTLRRWVA NLEGQWERAQ RLAGAGRARV WRLYMAASAL AFERNRIGVN QVLVVRTPEE
GASGLPLRAR AWDQAS
//
