ID   A1AK94_PELPD            Unreviewed;       430 AA.
AC   A1AK94;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ABK97764.1};
DE            EC=2.1.1.79 {ECO:0000313|EMBL:ABK97764.1};
GN   OrderedLocusNames=Ppro_0127 {ECO:0000313|EMBL:ABK97764.1};
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK97764.1, ECO:0000313|Proteomes:UP000006732};
RN   [1] {ECO:0000313|EMBL:ABK97764.1, ECO:0000313|Proteomes:UP000006732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC   {ECO:0000313|Proteomes:UP000006732};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
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DR   EMBL; CP000482; ABK97764.1; -; Genomic_DNA.
DR   RefSeq; WP_011734078.1; NC_008609.1.
DR   AlphaFoldDB; A1AK94; -.
DR   STRING; 338966.Ppro_0127; -.
DR   KEGG; ppd:Ppro_0127; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_0_2_7; -.
DR   OrthoDB; 9782855at2; -.
DR   Proteomes; UP000006732; Chromosome.
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:SF2; TUBERCULOSTEARIC ACID METHYLTRANSFERASE UFAA1; 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:ABK97764.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK97764.1}.
FT   ACT_SITE        394
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ   SEQUENCE   430 AA;  48829 MW;  E81455835B71330B CRC64;
     MNRNEQTCSS CPQTASTTNG IIDKLARSLV LNSLTAIRHG HLVLVDRDKR REFGRNDSEL
     TSTVRVQHPD FYRRVAFGGS IAAGESYMDG LWTCSDLTAL VRIMVRNQEA QQQLEGGLAR
     LTVPLQRLLH RLNDNTRTGS RRNIAAHYDL GNDFYQLFLD PTMAYSCGIF ERDNCTLEEA
     STAKFDRICR KLGLTADMKV LEIGTGWGGF AIHAARNYGC HVTTTTISQQ QHDLAAERIA
     AAGLAECITL LQRDYRDLTG QFDRLVSIEM IEAVGHRHLP TYFRICSDRL KPDGAALIQA
     ITMPDHHYGR YLKAPDFINR YIFPGSCCPS LHAISEAVAR ETDLRLTHLE DISLHYARTL
     REWSNAFHAN LEQVRGMGFD ERFIRMWEFY LCYCEGGFAE RFTGDLQLLF TKPVYRNESL
     LHPLKRSAPL
//