P0A9H7 (CFA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclopropane-fatty-acyl-phospholipid synthase
Short name=CFA synthase
Short name=Cyclopropane fatty acid synthase
EC=2.1.1.79

Gene names

Name:	cfa
Synonyms:	cdfA
Ordered Locus Names:	b1661, JW1653

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
Enzyme regulation	Inhibited by sinefungin, A9145C and S-adenosyl-L-homocysteine. Ref.1
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the CFA/CMAS family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway lipid modification Inferred from direct assay PubMed 6325391. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cyclopropane-fatty-acyl-phospholipid synthase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hrpB	P37024	1	EBI-1124838,EBI-549226

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 382	381	Cyclopropane-fatty-acyl-phospholipid synthase		PRO_0000089572
Regions
	Region	137 – 138	2	S-adenosyl-L-methionine binding By similarity
	Region	171 – 179	9	S-adenosyl-L-methionine binding By similarity
	Region	197 – 202	6	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	354	1	By similarity
Experimental info
	Sequence conflict	2	1	S → R in X69109. Ref.2
	Sequence conflict	8	1	E → G in X69109. Ref.2
	Sequence conflict	25	1	S → N in X69109. Ref.2
	Sequence conflict	39	1	I → T in X69109. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0A9H7 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 861FF3314FDAF2C4	FASTA	382	43,909
	10 20 30 40 50 60 MSSSCIEEVS VPDDNWYRIA NELLSRAGIA INGSAPADIR VKNPDFFKRV LQEGSLGLGE 70 80 90 100 110 120 SYMDGWWECD RLDMFFSKVL RAGLENQLPH HFKDTLRIAG ARLFNLQSKK RAWIVGKEHY 130 140 150 160 170 180 DLGNDLFSRM LDPFMQYSCA YWKDADNLES AQQAKLKMIC EKLQLKPGMR VLDIGCGWGG 190 200 210 220 230 240 LAHYMASNYD VSVVGVTISA EQQKMAQERC EGLDVTILLQ DYRDLNDQFD RIVSVGMFEH 250 260 270 280 290 300 VGPKNYDTYF AVVDRNLKPE GIFLLHTIGS KKTDLNVDPW INKYIFPNGC LPSVRQIAQS 310 320 330 340 350 360 SEPHFVMEDW HNFGADYDTT LMAWYERFLA AWPEIADNYS ERFKRMFTYY LNACAGAFRA 370 380 RDIQLWQVVF SRGVENGLRV AR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid sequence, purification, and studies of the enzyme active site." Wang A.-Y., Grogan D.W., Cronan J.E. Jr. Biochemistry 31:11020-11028(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9, ENZYME REGULATION. Strain: K12.
[2]	Eberhardt S.M.R., Richter G., Gimbel W., Werner T., Bacher A. Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / RR28.
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M98330 Genomic DNA. Translation: AAA23562.1. X69109 Genomic DNA. No translation available. U00096 Genomic DNA. Translation: AAC74733.1. AP009048 Genomic DNA. Translation: BAA15428.1.
PIR	A44292.
RefSeq	NP_416178.1. NC_000913.2. YP_489925.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A9H7.
SMR	P0A9H7. Positions 120-359.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48026N.
IntAct	P0A9H7. 2 interactions.
MINT	MINT-1312967.
STRING	511145.b1661.
Proteomic databases
PaxDb	P0A9H7.
PRIDE	P0A9H7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74733; AAC74733; b1661. BAA15428; BAA15428; BAA15428.
GeneID	12934382. 944811.
KEGG	ecj:Y75_p1638. eco:b1661.
PATRIC	32118628. VBIEscCol129921_1734.
Organism-specific databases
EchoBASE	EB1493.
EcoGene	EG11531. cfa.
Phylogenomic databases
eggNOG	COG2230.
HOGENOM	HOG000245194.
KO	K00574.
OMA	LMLDPYM.
ProtClustDB	PRK11705.
Enzyme and pathway databases
BioCyc	EcoCyc:CFA-MONOMER. ECOL316407:JW1653-MONOMER. MetaCyc:CFA-MONOMER.
SABIO-RK	P0A9H7.
UniPathway	UPA00094.
Gene expression databases
Genevestigator	P0A9H7.
Family and domain databases
InterPro	IPR003333. Mycolic_cyclopropane_synthase. [Graphical view]
Pfam	PF02353. CMAS. 1 hit. [Graphical view]
PIRSF	PIRSF003085. CMAS. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CFA_ECOLI

Accession

Primary (citable) accession number: P0A9H7
Secondary accession number(s): P30010

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program