ID A0A087A1Y2_9BIFI Unreviewed; 368 AA.
AC A0A087A1Y2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:KFI52782.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:KFI52782.1};
GN ORFNames=BBIA_0467 {ECO:0000313|EMBL:KFI52782.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI52782.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI52782.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI52782.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-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:KFI52782.1}.
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DR EMBL; JGYN01000004; KFI52782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087A1Y2; -.
DR STRING; 1437608.GCA_000771645_02329; -.
DR eggNOG; COG2230; Bacteria.
DR Proteomes; UP000029108; 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:KFI52782.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029108};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFI52782.1}.
FT ACT_SITE 330
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 368 AA; 41552 MW; 05D65F5EEDCFA33F CRC64;
MLGDFDIDGI DYADPYPQLR QLLSLAPYVR PLSPLSVAKV AGSILSHGIR KAPVPATEGP
SKFARIKSGL LPHTEKADSE TVSFHYDLSN GFYRNFLGPT MTYTCAVFPS EETSLEDAQL
NKIRLVLDKL GLKPGDRLLD IGCGWGSLVI EAAKRGIKAL GVSLSKEQIE YGQEWIKREG
LEDLAELRVM DYRDVPERDF DGICSIGMME HVGVKNYQSY FEEMFKLLKP CGRLLNHQIT
ISHDKPNGKP GTDEFLDRYI FPDGDLGAPG FIESCIHDAG FNVVHQENLR QHYALTLHHW
NRNLSAHWEE AVQEVGFERA KVWGLYMAAC ALNFEIDGIQ VHQFLAVKPD RVGHPDGKWY
PLRPWWRA
//
