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Database: UniProt
Entry: C6LI48_9FIRM
LinkDB: C6LI48_9FIRM
Original site: C6LI48_9FIRM 
ID   C6LI48_9FIRM            Unreviewed;       390 AA.
AC   C6LI48;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:EET59703.1};
DE            EC=2.1.1.79 {ECO:0000313|EMBL:EET59703.1};
GN   ORFNames=BRYFOR_08319 {ECO:0000313|EMBL:EET59703.1};
OS   Marvinbryantia formatexigens DSM 14469.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Marvinbryantia.
OX   NCBI_TaxID=478749 {ECO:0000313|EMBL:EET59703.1, ECO:0000313|Proteomes:UP000005561};
RN   [1] {ECO:0000313|EMBL:EET59703.1, ECO:0000313|Proteomes:UP000005561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14469 {ECO:0000313|EMBL:EET59703.1,
RC   ECO:0000313|Proteomes:UP000005561};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2009) 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:EET59703.1}.
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DR   EMBL; ACCL02000016; EET59703.1; -; Genomic_DNA.
DR   RefSeq; WP_006863096.1; NZ_CP102268.1.
DR   AlphaFoldDB; C6LI48; -.
DR   STRING; 168384.SAMN05660368_02613; -.
DR   eggNOG; COG2230; Bacteria.
DR   OrthoDB; 9782855at2; -.
DR   Proteomes; UP000005561; 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; 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   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:EET59703.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EET59703.1}.
FT   ACT_SITE        360
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ   SEQUENCE   390 AA;  45309 MW;  82B441C7DC229730 CRC64;
     MLEKAEEKAM VQFLDRFDEH PFRLKFSDSE YMVGTGEPEF TVCFKKAIPV ADLLRSTSIA
     LGEAYMDGDL EIEGNLYEAL DCFLGQMGKF STDEKALKKI IHSSVTKKQQ KQEVSSHYDI
     GNDFYSLWLD KTMSYSCAYF KNPDDSLYQA QKNKVDYILQ KLYLKEGMTL LDIGCGWGFL
     LIEAAKKYKI KGLGITLSNE QYVKFQQTIK DEGLEDYLEV KLMDYRDLPG LGRQFDRVVS
     VGMVEHVGRE NYQLFNDCVS RVLKNGGLYL LHFISALKEH PGDAWIKKYI FPGGMVPSLR
     EMLSCAAEDN FHTLDVENLR LHYNRTLLCW EKNFREHIDE VRQMFDERFV RMWDLYLSAC
     AATFHNGIID IHQILFTKGI NNELPMTRWF
//
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