ID A9WVG7_RENSM Unreviewed; 419 AA.
AC A9WVG7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ABY25188.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:ABY25188.1};
GN OrderedLocusNames=RSal33209_3479 {ECO:0000313|EMBL:ABY25188.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY25188.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000910; ABY25188.1; -; Genomic_DNA.
DR RefSeq; WP_012246816.1; NC_010168.1.
DR AlphaFoldDB; A9WVG7; -.
DR STRING; 288705.RSal33209_3479; -.
DR KEGG; rsa:RSal33209_3479; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_0_2_11; -.
DR Proteomes; UP000002007; 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:ABY25188.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABY25188.1}.
SQ SEQUENCE 419 AA; 46870 MW; 923903EBDFB8C3DF CRC64;
MTHTIPTAKV RADLWPDVAM PPSSFRARAG QPIAGSLFRA AVKRLPILVA QPDGSTMGLG
GPRMDLREPD SFYARIAHNG LIGLGESYMA REWEAEDLAA LMTVFASKVS KLIPQPLQTL
RGALLPHQPQ RERNTEGNSR NNISRHYDLS NELFAEFLDE TMSYSSAYFV DLDQPGFDRL
ASAQEAKIDR LLDLAGVTEG TRLLEIGTGW GELALRAARR GAQVYSVTLS SEQKELAEDR
IQSAGFADSV QIELLDYRKV EGTFDAIVSV EMIEAVGFEF MPEYFRTLSA RLKPGGAIGL
QAITIGHERM LATRNSYTWV HKYIFPGGMI PSAELISEQS SLNGLRVENR LAFGQHYAQT
LRLWDEQFAR NAGKVDELGF DETFRRMWHF YLAYSRAGFA SGYLDVQQFQ LRKAKENNS
//
