ID A0A086ZFV8_9BIFI Unreviewed; 441 AA.
AC A0A086ZFV8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:KFI45408.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:KFI45408.1};
GN ORFNames=BBOH_1183 {ECO:0000313|EMBL:KFI45408.1};
OS Bifidobacterium bohemicum DSM 22767.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437606 {ECO:0000313|EMBL:KFI45408.1, ECO:0000313|Proteomes:UP000029096};
RN [1] {ECO:0000313|EMBL:KFI45408.1, ECO:0000313|Proteomes:UP000029096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22767 {ECO:0000313|EMBL:KFI45408.1,
RC ECO:0000313|Proteomes:UP000029096};
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:KFI45408.1}.
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DR EMBL; JGYP01000002; KFI45408.1; -; Genomic_DNA.
DR RefSeq; WP_044098085.1; NZ_JGYP01000002.1.
DR AlphaFoldDB; A0A086ZFV8; -.
DR STRING; 1437606.BBOH_1183; -.
DR eggNOG; COG2230; Bacteria.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000029096; 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:KFI45408.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029096};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFI45408.1}.
FT ACT_SITE 391
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 441 AA; 49940 MW; 82ED418A26775BE2 CRC64;
MASMSVAEMI GLFLNDNGKV NFEAFDGSSL GPKDAPLHIH VNNSRAVYYM VDHPNDLGLA
RAYLQGDISS PELIPGDPYV VFKELMALKP DLKRPNPADL ARILSSVYSH GIRHPEPPSI
EGPSRWRRRA EGLMPHSKAG DSATVSYHYD QSNEFYRLFL GSSMTYTCAV FDTPEDSLED
AEWRKLDLVL DKLNLKPGDR LLDIGCGWGS MEIRAAQRGI KVLGVTLAGE QVKWAQEWIK
REGLEDLAEV RQMDYRDVPE GDFDGICSLG MMEHVGFKHY PSYFQEIFDK LKPNGRLLNH
QITRVNSKTG KSAGEFIDRY IFPDGQLASP GEIETVIHDT GFEVVNQENL RQHYALTLHH
WNKNLVAGWD RAVELMGEPK ARLWGLYMAG CALNFELNNI QIHQFLCVRP DDTKMTDHYP
LRPWWVKDSE VLPTQVEAPK A
//