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Database: UniProt
Entry: A0A1E4K014_9PROT
LinkDB: A0A1E4K014_9PROT
Original site: A0A1E4K014_9PROT 
ID   A0A1E4K014_9PROT        Unreviewed;       445 AA.
AC   A0A1E4K014;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ODU32590.1};
GN   ORFNames=ABS93_00110 {ECO:0000313|EMBL:ODU32590.1};
OS   Thiobacillus sp. SCN 62-729.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1660148 {ECO:0000313|EMBL:ODU32590.1, ECO:0000313|Proteomes:UP000094151};
RN   [1] {ECO:0000313|EMBL:ODU32590.1, ECO:0000313|Proteomes:UP000094151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
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:ODU32590.1}.
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DR   EMBL; MEFL01000002; ODU32590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4K014; -.
DR   Proteomes; UP000094151; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   ACT_SITE        405
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ   SEQUENCE   445 AA;  51160 MW;  9F920BE1A6BF8FE3 CRC64;
     MTTSTEMALP PAIPGIELAK HILHRLFRDF DGCLRIRLWD GSEVHLGHNH PAFSLSFRSS
     KAFQELILAR DPLRLAESYF QGRIDIDGDL YSALKLRHHL ASLKLSLMEK AELAAKAFRI
     KLEKTASTSS DTPKWEKTFG QKMGLEPSKD LNRHAISFHY DVSNDFYTLW LDEQMVYSCA
     YYEDASQSLE QAQRDKLDHI CRKLRLKPGE RLLDIGCGWG ALICWAAEHY GVSAYGITLS
     QNQYDHAQRT IKQRGLEHKV SVELLDYRDL QGEARFDKLV SVGMFEHVGL KNLPTYFAIA
     NRLLKPGGLF LNHGITSDEG GWKKTVSTEF INRYIFPDGQ LETVSTVQKI MEDTGFEVHD
     VEGLRQHYAL TLREWVRRLD ARHEEALNYV TEPVYRVWRL YMAACAMQFE EGNTGIYQIL
     ASRREPFSSP VPLTRRDLYR QPGIK
//
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