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InterPro: IPR003333 Cyclopropane-fatty-acyl-phospholipid synthase

Protein matches Help

UniProtKB

Matches:

1837 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003333 CMAS

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02353	CMAS	1837
PIRSF	PIRSF003085	CMAS	1461
Signatures in BioMart

GO Term annotation Help

Process

GO:0008610 lipid biosynthetic process

Function

GO:0008825 cyclopropane-fatty-acyl-phospholipid synthase activity

InterPro annotation

Entry Details in BioMart

Abstract

Methyl transfer from the ubiquitous S-adenosyl-L-methionine (AdoMet) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalyzed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as catechol for regulatory purposes. The various aspects of the role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.

This entry represents cyclopropane-fatty-acyl-phospholipid synthase that is slosely related to methyltransferases.

Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 catalyses the reaction:

S-adenosyl-L-methionine + phospholipid olefinic fatty acid -> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.

The major mycolic acid produced by Mycobacterium tuberculosis contains two cis-cyclopropanes in the meromycolate chain. Cyclopropanation may contribute to the structural integrity of the cell wall complex [1].

Structural links Help

PDB - click here

SCOP: c.66.1.18

CATH: 3.40.50.150

Database links Help

Enzyme: EC:2.1.1

PANDIT: PF02353

Blocks: IPB003333

Pfam Clan: CL0102.19

AC	CL0102.19
ID	Methyltransfer
DE	Methyltransferase superfamily
PF00145	IPR001525	DNA methylase, C-5 cytosine-specific
PF00398	IPR001737	Ribosomal RNA adenine methylase transferase
PF00891	IPR001077	O-methyltransferase, family 2
PF01135	IPR000682	Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PF01170	IPR000241	Putative RNA methylase
PF01189	IPR001678	Bacterial Fmu (Sun)/eukaryotic nucleolar NOL1/Nop2p
PF01209	IPR004033	UbiE/COQ5 methyltransferase
PF01234	IPR000940	Methyltransferase, NNMT/PNMT/TEMT
PF01269	IPR000692	Fibrillarin
PF01358	IPR000176	Poly A polymerase regulatory subunit
PF01555	IPR002941	DNA methylase N-4/N-6
PF01564	IPR001045	Spermine synthase
PF01596	IPR002935	O-methyltransferase, family 3
PF01728	IPR002877	Ribosomal RNA methyltransferase RrmJ/FtsJ
PF01739	IPR000780	MCP methyltransferase, CheR-type
PF01795	IPR002903	S-adenosyl-L-methionine-dependent methyltransferase, MraW
PF01861	IPR002723	Protein of unknown function DUF43
PF02005	IPR002905	N2,N2-dimethylguanosine tRNA methyltransferase
PF02086	IPR012327	D12 class N6 adenine-specific DNA methyltransferase
PF02353	IPR003333	Cyclopropane-fatty-acyl-phospholipid synthase
PF02384	IPR003356	DNA methylase, adenine-specific
PF02390	IPR003358	tRNA (guanine-N-7) methyltransferase
PF02475	IPR003402	Protein of unknown function Met10
PF02527	IPR003682	rRNA small subunit methyltransferase G
PF03141	IPR004159	Protein of unknown function DUF248, methyltransferase putative
PF03269	IPR004951	Protein of unknown function DUF268, Caenorhabditis species
PF03291	IPR004971	mRNA capping enzyme, large subunit
PF03602	IPR004398	Conserved hypothetical protein CHP00095
PF03848	IPR015985	Tellurite resistance methyltransferase, TehB, core
PF04378	IPR007473	Protein of unknown function DUF519
PF04445	IPR007536	Protein of unknown function DUF548
PF04672	IPR006764	Protein of unknown function DUF574
PF04816	IPR006901	Protein of unknown function DUF633
PF05063	IPR007757	MT-A70
PF05148	IPR007823	Methyltransferase-related
PF05175	IPR007848	Methyltransferase small
PF05219	IPR007884	DREV methyltransferase
PF05401	IPR008715	Nodulation protein S, NodS-related
PF05430	IPR008471	Protein of unknown function DUF752
PF05724	IPR008854	Thiopurine S-methyltransferase
PF05891	IPR008576	Protein of unknown function DUF858, methyltransferase-like
PF05958	IPR010280	(Uracil-5)-methyltransferase
PF05971	IPR010286	S-adenosyl-L-methionine dependent methyltransferase, predicted
PF06080	IPR010342	Protein of unknown function DUF938
PF06325	IPR010456	Ribosomal L11 methyltransferase
PF06460	IPR009461	Coronavirus NSP13
PF06859	IPR010675	Bicoid-interacting 3
PF06962	IPR010719	Putative rRNA methylase
PF07021	IPR010743	Methionine biosynthesis MetW
PF07109	IPR010940	Magnesium-protoporphyrin IX methyltransferase, C-terminal
PF07279	IPR009902	Protein of unknown function DUF1442
PF07669	IPR011639	Restriction endonuclease, Eco57I
PF07757	IPR011671	AdoMet-dependent methyltransferase, predicted
PF07942	IPR012901	N2227-like
PF08003	IPR010017	tRNA (mo5U34)-methyltransferase
PF08123	IPR013110	Histone methylation DOT1
PF08241	IPR013216	Methyltransferase type 11
PF08242	IPR013217	Methyltransferase type 12
PF08704	IPR014816	tRNA methyltransferase complex GCD14 subunit
PF09243	IPR015324	Ribosomal protein Rsm22, bacterial-type
PF09445	IPR019012	RNA cap guanine-N2 methyltransferase
PF10294	IPR019410	Methyltransferase-16, putative
PF10672	IPR019614	S-adenosylmethionine-dependent methyltransferase

Taxonomic coverage Help

Example proteins Help

P0A5P0 Cyclopropane-fatty-acyl-phospholipid synthase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003333	Cyclopropane-fatty-acyl-phospholipid synthase
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	George KM, Yuan Y, Sherman DR, Barry CE 3rd. The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2. J. Biol. Chem. 270 27292-8 1995 [PubMed: 7592990] http://dx.doi.org/10.1074/jbc.270.45.27292

Additional Reading Open in usermanual
	Boissier F, Bardou F, Guillet V, Uttenweiler-Joseph S, Daffe M, Quemard A, Mourey L. Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. J. Biol. Chem. 281 2006 4434-45 [PubMed: 16356931] http://dx.doi.org/10.1074/jbc.M510250200
	Huang CC, Smith CV, Glickman MS, Jacobs WR Jr, Sacchettini JC. Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis. J. Biol. Chem. 277 2002 11559-69 [PubMed: 11756461] http://dx.doi.org/10.1074/jbc.M111698200
	Yuan Y, Barry CE 3rd. A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 93 1996 12828-33 [PubMed: 8917504] http://dx.doi.org/10.1073/pnas.93.23.12828

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