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P0A954 (FABB_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 63. 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:
3-oxoacyl-[acyl-carrier-protein] synthase 1

EC=2.3.1.41
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase I
Beta-ketoacyl-ACP synthase I
Short name=KAS I
Gene names
Name:fabB
Ordered Locus Names:c2869
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids By similarity.

Catalytic activity

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
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_function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4064063-oxoacyl-[acyl-carrier-protein] synthase 1
PRO_0000180312

Sites

Active site1631 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A954 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 489D8BAD23E78113

FASTA40642,613
        10         20         30         40         50         60 
MKRAVITGLG IVSSIGNNQQ EVLASLREGR SGITFSQELK DSGMRSHVWG NVKLDTTGLI 

        70         80         90        100        110        120 
DRKVVRFMSD ASIYAFLSME QAIADAGLSP EAYQNNPRVG LIAGSGGGSP RFQVFGADAM 

       130        140        150        160        170        180 
RGPRGLKAVG PYVVTKAMAS GVSACLATPF KIHGVNYSIS SACATSAHCI GNAVEQIQLG 

       190        200        210        220        230        240 
KQDIVFAGGG EELCWEMACE FDAMGALSTK YNDTPEKASR TYDAHRDGFV IAGGGGMVVV 

       250        260        270        280        290        300 
EELEHALARG AHIYAEIVGY GATSDGADMV APSGEGAVRC MKMAMHGVDT PIDYLNSHGT 

       310        320        330        340        350        360 
STPVGDVKEL AAIREVFGDK SPAISATKAM TGHSLGAAGV QEAIYSLLML EHGFIAPSIN 

       370        380        390        400 
IEELDEQAAG LNIVTETTDR ELTTVMSNSF GFGGTNATLV MRKLKD 

« 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: AAN81319.1.
RefSeqNP_754751.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0A954.
SMRP0A954. Positions 1-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2869.

Chemistry

BindingDBP0A954.

Proteomic databases

PRIDEP0A954.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN81319; AAN81319; c2869.
GeneID1038429.
KEGGecc:c2869.
PATRIC18283598. VBIEscCol75197_2706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000060165.
KOK00647.
OMAIGNNTQE.
OrthoDBEOG6DG2SR.
ProtClustDBPRK07967.

Enzyme and pathway databases

BioCycECOL199310:C2869-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
InterProIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 2 hits.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABB_ECOL6
AccessionPrimary (citable) accession number: P0A954
Secondary accession number(s): P14926 expand/collapse secondary AC list , Q9R828, Q9R829, Q9R830
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: December 11, 2013
This is version 63 of the entry and version 1 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