ID W3Y024_9FIRM Unreviewed; 390 AA.
AC W3Y024;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ETS91583.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:ETS91583.1};
GN ORFNames=HMPREF1521_1234 {ECO:0000313|EMBL:ETS91583.1};
OS Veillonella sp. AS16.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=936589 {ECO:0000313|EMBL:ETS91583.1, ECO:0000313|Proteomes:UP000019042};
RN [1] {ECO:0000313|EMBL:ETS91583.1, ECO:0000313|Proteomes:UP000019042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS16 {ECO:0000313|EMBL:ETS91583.1,
RC ECO:0000313|Proteomes:UP000019042};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) 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:ETS91583.1}.
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DR EMBL; AZYX01000022; ETS91583.1; -; Genomic_DNA.
DR RefSeq; WP_038118176.1; NZ_AZYX01000022.1.
DR AlphaFoldDB; W3Y024; -.
DR PATRIC; fig|936589.3.peg.1676; -.
DR eggNOG; COG2230; Bacteria.
DR Proteomes; UP000019042; 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:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ETS91583.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETS91583.1}.
FT ACT_SITE 360
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 390 AA; 45155 MW; 39F6A1D5AA54976D CRC64;
MFSKLFDSFL VHYLERFNDH CFTVKIGDNE YTIGDGESEF TVIVNRDIPK KDLLISAELA
LGEAYMRKDI EIKGDLFKAL CVVLGHVGKD SINRKVLSSL FNAGLKKKDQ KQQVSSHYDL
GNEFYKLWLD ETMSYSCAYF KHDDDSLKDA QYQKVHHILD KLYLKEGMTL LDIGCGWGFL
LIEAARKYGV KGYGCTLSEE QWKKGQERIK EYALEGQVEI ELIDYRDVAA SGRTFDRIVS
IGMLEHVGRA NFPLYMEDAS DMLKDGGLFL LHYISDPSEK ETSAWIRKYI FPGGCLPSLR
EMVSLAYDYD MNVIDVESLR YHYYKTLMHW YNNFQGVREQ VEAKRGSEFV RMWDLYLCGC
AAGFYIGNMD LHQILMTKGI TNELPLTRWY
//