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P0A9H7 (CFA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processLipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lipid modification

Inferred from direct assay PubMed 6325391. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclopropane-fatty-acyl-phospholipid synthase activity

Inferred from direct assay Ref.1. Source: EcoCyc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

hrpBP370241EBI-1124838,EBI-549226

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 382381Cyclopropane-fatty-acyl-phospholipid synthase
PRO_0000089572

Regions

Region137 – 1382S-adenosyl-L-methionine binding By similarity
Region171 – 1799S-adenosyl-L-methionine binding By similarity
Region197 – 2026S-adenosyl-L-methionine binding By similarity

Sites

Active site3541 By similarity

Experimental info

Sequence conflict21S → R in X69109. Ref.2
Sequence conflict81E → G in X69109. Ref.2
Sequence conflict251S → N in X69109. Ref.2
Sequence conflict391I → T in X69109. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0A9H7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 861FF3314FDAF2C4

FASTA38243,909
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 277:1453-1462(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.
PIRA44292.
RefSeqNP_416178.1. NC_000913.3.
YP_489925.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A9H7.
SMRP0A9H7. Positions 120-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48026N.
IntActP0A9H7. 2 interactions.
MINTMINT-1312967.
STRING511145.b1661.

Proteomic databases

PaxDbP0A9H7.
PRIDEP0A9H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74733; AAC74733; b1661.
BAA15428; BAA15428; BAA15428.
GeneID12934382.
944811.
KEGGecj:Y75_p1638.
eco:b1661.
PATRIC32118628. VBIEscCol129921_1734.

Organism-specific databases

EchoBASEEB1493.
EcoGeneEG11531. cfa.

Phylogenomic databases

eggNOGCOG2230.
HOGENOMHOG000245194.
KOK00574.
OMAASEPHFV.
OrthoDBEOG6BGNZP.
PhylomeDBP0A9H7.
ProtClustDBPRK11705.

Enzyme and pathway databases

BioCycEcoCyc:CFA-MONOMER.
ECOL316407:JW1653-MONOMER.
MetaCyc:CFA-MONOMER.
SABIO-RKP0A9H7.
UniPathwayUPA00094.

Gene expression databases

GenevestigatorP0A9H7.

Family and domain databases

InterProIPR003333. Mycolic_cyclopropane_synthase.
[Graphical view]
PfamPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFPIRSF003085. CMAS. 1 hit.
ProtoNetSearch...

Other

PROP0A9H7.

Entry information

Entry nameCFA_ECOLI
AccessionPrimary (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: April 16, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene