ID C1B4F6_RHOOB Unreviewed; 430 AA.
AC C1B4F6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Putative cyclopropane fatty acid synthase {ECO:0000313|EMBL:BAH55145.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:BAH55145.1};
GN Name=cfa {ECO:0000313|EMBL:BAH55145.1};
GN OrderedLocusNames=ROP_68980 {ECO:0000313|EMBL:BAH55145.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH55145.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH55145.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH55145.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH55145.1; -; Genomic_DNA.
DR RefSeq; WP_015890575.1; NC_012522.1.
DR AlphaFoldDB; C1B4F6; -.
DR STRING; 632772.ROP_68980; -.
DR KEGG; rop:ROP_68980; -.
DR PATRIC; fig|632772.20.peg.7189; -.
DR HOGENOM; CLU_026434_6_2_11; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000002212; 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:BAH55145.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAH55145.1}.
SQ SEQUENCE 430 AA; 46593 MW; A1EFAFD380F6B3A5 CRC64;
MTVADTVAPL VRAVLGTQVP VGIRCWDGSR SGPPDAPWQV HLVNRRGLRR LLWAPNDLGF
ARAYVSGDID IEGDLLAGLD ALEEVADPSR GPGVRIDGQT KKALVTAALR LGIVGLPPKP
PAEEMKLARG RRHDKARDAA AISHHYDVGN DFYRLVLGES MTYSCAYWAE PGGDLDAAQY
AKCDLVARKL GLTAGMRVLD VGCGWGTFAL HAARHYGVHV VGVTLSHEQA DYAAKRMVDA
GVGELVQIRV QDYRDVADGP YDAISSIGMA EHVGDAMLAT YAADLFALLR PQGRLLNHAI
SRRPRESADT FSSTSFIDRY VFPDGEIEPM APMIDALEGA GFEVRDVESL REHYALTLRA
WVANLEANWD EAVAASSAGR ARVWRLYMAG AALAFSANRL GINQILAVRS TERGDSGMPG
TRDELLRAHT
//
