Tag | Content |
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CPLM ID | CPLM-003174 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cyclopropane-fatty-acyl-phospholipid synthase |
Protein Synonyms/Alias | CFA synthase; Cyclopropane fatty acid synthase |
Gene Name | cfa |
Gene Synonyms/Alias | cdfA; b1661; JW1653 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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42 | APADIRVKNPDFFKR | acetylation | [1] | 117 | KRAWIVGKEHYDLGN | acetylation | [1] | 258 | AVVDRNLKPEGIFLL | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge (By similarity). |
Sequence Annotation | REGION 137 138 S-adenosyl-L-methionine binding (By REGION 171 179 S-adenosyl-L-methionine binding (By REGION 197 202 S-adenosyl-L-methionine binding (By ACT_SITE 354 354 By similarity. |
Keyword | Complete proteome; Cytoplasm; Direct protein sequencing; Lipid biosynthesis; Lipid metabolism; Methyltransferase; Reference proteome; S-adenosyl-L-methionine; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 382 AA |
Protein Sequence | MSSSCIEEVS VPDDNWYRIA NELLSRAGIA INGSAPADIR VKNPDFFKRV LQEGSLGLGE 60 SYMDGWWECD RLDMFFSKVL RAGLENQLPH HFKDTLRIAG ARLFNLQSKK RAWIVGKEHY 120 DLGNDLFSRM LDPFMQYSCA YWKDADNLES AQQAKLKMIC EKLQLKPGMR VLDIGCGWGG 180 LAHYMASNYD VSVVGVTISA EQQKMAQERC EGLDVTILLQ DYRDLNDQFD RIVSVGMFEH 240 VGPKNYDTYF AVVDRNLKPE GIFLLHTIGS KKTDLNVDPW INKYIFPNGC LPSVRQIAQS 300 SEPHFVMEDW HNFGADYDTT LMAWYERFLA AWPEIADNYS ERFKRMFTYY LNACAGAFRA 360 RDIQLWQVVF SRGVENGLRV AR 382 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IDA:EcoCyc. GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. GO:0030258; P:lipid modification; IDA:EcoCyc. |
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