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Database: UniProt
Entry: A0A069ICS5_9BURK
LinkDB: A0A069ICS5_9BURK
Original site: A0A069ICS5_9BURK 
ID   A0A069ICS5_9BURK        Unreviewed;       404 AA.
AC   A0A069ICS5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:KDP87293.1};
GN   ORFNames=CF70_002110 {ECO:0000313|EMBL:KDP87293.1};
OS   Cupriavidus sp. SK-3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP87293.1, ECO:0000313|Proteomes:UP000023560};
RN   [1] {ECO:0000313|EMBL:KDP87293.1, ECO:0000313|Proteomes:UP000023560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-3 {ECO:0000313|EMBL:KDP87293.1,
RC   ECO:0000313|Proteomes:UP000023560};
RA   Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT   "Cupriavidus sp. strain SK-3.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KDP87293.1}.
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DR   EMBL; JFJV02000109; KDP87293.1; -; Genomic_DNA.
DR   RefSeq; WP_035864521.1; NZ_JFJV02000109.1.
DR   AlphaFoldDB; A0A069ICS5; -.
DR   OrthoDB; 9782855at2; -.
DR   Proteomes; UP000023560; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   ACT_SITE        384
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ   SEQUENCE   404 AA;  45401 MW;  CADAE4D01D39DA05 CRC64;
     MTPSRALTLP PDGAPASARL FLTLLERICV GHLLLVTPAG EQRLFGDPHG GPGARLELHD
     WRACGEILRA GDIGFAEAYR AGWVDSPDLT ALLRLAIRNE PALPQTVVGS WLARLWYGLR
     HVLRPNSRQG SRRNIHAHYD LGNAFYQRWL DPSWTYSAAL FQGEKNRSLE TAQYAKYQHI
     VNTLALKPGM RVLEVGCGWG GFALHAARQG IQVHGITISV AQLEVARRRV VEAGLEGLAR
     LELRDYRDVD GEYDAIVSIE MFEAVGERYW PSYFGMLRQR LRPGARALVQ SITIAEQRFE
     AYRASSDFIR EYVFPGGMLP SPRRFLRAAL QAGMDGRATL AFGSDYAQTL RHWRAAFEQA
     LDDIAAQGFD NTFVRTWRLY LCYCEAGFDE GRTDVMQFVL QRAG
//
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