ID A1VLG3_POLNA Unreviewed; 421 AA.
AC A1VLG3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ABM36491.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:ABM36491.1};
GN OrderedLocusNames=Pnap_1175 {ECO:0000313|EMBL:ABM36491.1};
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM36491.1, ECO:0000313|Proteomes:UP000000644};
RN [1] {ECO:0000313|Proteomes:UP000000644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP000529; ABM36491.1; -; Genomic_DNA.
DR RefSeq; WP_011800584.1; NC_008781.1.
DR AlphaFoldDB; A1VLG3; -.
DR STRING; 365044.Pnap_1175; -.
DR KEGG; pna:Pnap_1175; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_6_2_4; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000000644; 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: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:ABM36491.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABM36491.1}.
SQ SEQUENCE 421 AA; 46537 MW; 1752A2653B656E0B CRC64;
MFQSLVPGHP SHLSGLPPEI ALQLPQGQQL GAADAPVRLS FSRWSSIARL KAGQIGALAE
DYVEGKLQLE GAMRDVMRAT LKLLPGNPVE SDTGWWTALR HRAKSLTAHT LARDATQIQF
HYDVSDAFYA LWLDPRRVYS CAYYRETGMT LAQAQEAKLD HICRKLMLQP GEHFLDIGAG
WGGLLLWAAE HYGVDATGIT LSKNQHAHVQ QLIDAKGLGQ RVRIELCDYR DLPEKKPFDK
ISSVGMFEHV GQVNMDAYFG KVMRLLAPGG LALNHGITAG GVDNRQLGAG MGDFIGKYIF
PGGELLHISA VLGHMAHSGL EMVDTENLRP HYGRTLWDWS DALEARLDEA RAVLAADGGL
ERAEKILRAY RLYLAGSAMS FEQGWIALHQ VLAARPALDR QGETIKGAQS AYPFNREFMY
R
//
