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P0A9H8 (CFA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Ordered Locus Names:c2055
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Cytoplasm Probable.

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
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclopropane-fatty-acyl-phospholipid synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 382381Cyclopropane-fatty-acyl-phospholipid synthase
PRO_0000089571

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

Sequences

Sequence LengthMass (Da)Tools
P0A9H8 [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

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN80515.1.
RefSeqNP_753950.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0A9H8.
SMRP0A9H8. Positions 120-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2055.

Proteomic databases

PRIDEP0A9H8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN80515; AAN80515; c2055.
GeneID1036202.
KEGGecc:c2055.
PATRIC18282011. VBIEscCol75197_1924.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000245194.
KOK00574.
OMAASEPHFV.
OrthoDBEOG6BGNZP.
ProtClustDBPRK11705.

Enzyme and pathway databases

BioCycECOL199310:C2055-MONOMER.
SABIO-RKP0A9H8.
UniPathwayUPA00094.

Family and domain databases

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

Entry information

Entry nameCFA_ECOL6
AccessionPrimary (citable) accession number: P0A9H8
Secondary accession number(s): P30010
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 61 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