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P0A953 (FABB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:fabC
Ordered Locus Names:b2323, JW2320
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.6

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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4064063-oxoacyl-[acyl-carrier-protein] synthase 1
PRO_0000180311

Sites

Active site1631

Natural variations

Natural variant41A → T in strain: MA-1 / fabB3.
Natural variant1401S → F in strain: K1060 / fabB5.
Natural variant2991G → S in strain: MA-1 / fabB3.
Natural variant3291A → V in strain: M5 / fabB15.

Secondary structure

.............................................................................. 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A953 [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

« Hide 'large scale' references
[1]"Beta-ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue."
Kauppinen S., Siggaard-Andersen M., von Wettstein-Knowles P.
Carlsberg Res. Commun. 53:357-370(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 158-168.
Strain: B.
[2]"Catalytic residues of beta-ketoacyl-ACP synthases."
Siggaard-Andersen M., von Wettstein-Knowles P., Gotthardt-Olsen J., Bangera G., Chuck J.-A., Pontoppidan B.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K1060 / fabB5, M5 / fabB15 and MA-1 / fabB3.
[3]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [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.
[6]"Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis."
Siggaard-Andersen M.
Carlsberg Res. Commun. 53:371-379(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UNSATURATED FATTY ACID SYNTHESIS.
[7]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[8]"The X-ray crystal structure of beta-ketoacyl [acyl carrier-protein] synthase I."
Olsen J.G., Kadziola A., von Wettstein-Knowles P., Siggaard-Andersen M., Lindquist Y., Larsen S.
FEBS Lett. 460:46-52(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24427 Genomic DNA. Translation: AAC67304.1.
AJ012161 Genomic DNA. Translation: CAA09932.1.
AJ012162 Genomic DNA. Translation: CAA09933.1.
AJ012163 Genomic DNA. Translation: CAA09934.1.
U00096 Genomic DNA. Translation: AAC75383.1.
AP009048 Genomic DNA. Translation: BAA16180.1.
PIRSYECA1. A31284.
RefSeqNP_416826.1. NC_000913.3.
YP_490565.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DD8X-ray2.30A/B/C/D1-406[»]
1EK4X-ray1.85A/B/C/D1-406[»]
1F91X-ray2.40A/B/C/D1-406[»]
1FJ4X-ray2.35A/B/C/D1-406[»]
1FJ8X-ray2.27A/B/C/D1-406[»]
1G5XX-ray2.45A/B/C/D1-406[»]
1H4FX-ray2.00A/B/C/D1-406[»]
2AQ7X-ray2.30A/B/C/D1-406[»]
2AQBX-ray2.19A/B/C/D1-406[»]
2BUHX-ray1.90A/B/C/D1-406[»]
2BUIX-ray2.40A/B/C/D1-406[»]
2BYWX-ray1.70A/B/C/D5-406[»]
2BYXX-ray2.00A/B/C/D5-406[»]
2BYYX-ray2.20A/B/C/D1-406[»]
2BYZX-ray1.95A/B/C/D1-406[»]
2BZ3X-ray2.00A/B/C/D1-406[»]
2BZ4X-ray1.86A/B/C/D1-406[»]
2CDHX-ray4.20A/B/C/D/E/F1-406[»]
2CF2X-ray4.30A/J1-406[»]
2VB7X-ray1.60A/B/C/D1-406[»]
2VB8X-ray1.52A/B/C/D1-406[»]
2VB9X-ray1.50A/B/C/D1-406[»]
2VBAX-ray1.36A/B/C/D1-406[»]
ProteinModelPortalP0A953.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29379N.
IntActP0A953. 9 interactions.
MINTMINT-1235843.
STRING511145.b2323.

Chemistry

BindingDBP0A953.
ChEMBLCHEMBL4913.
DrugBankDB01034. Cerulenin.

Proteomic databases

PaxDbP0A953.
PRIDEP0A953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75383; AAC75383; b2323.
BAA16180; BAA16180; BAA16180.
GeneID12931799.
946799.
KEGGecj:Y75_p2289.
eco:b2323.
PATRIC32120019. VBIEscCol129921_2419.

Organism-specific databases

EchoBASEEB0270.
EcoGeneEG10274. fabB.

Phylogenomic databases

eggNOGCOG0304.
HOGENOMHOG000060165.
KOK00647.
OMAFNPEYAE.
OrthoDBEOG6DG2SR.
PhylomeDBP0A953.

Enzyme and pathway databases

BioCycEcoCyc:FABB-MONOMER.
ECOL316407:JW2320-MONOMER.
MetaCyc:FABB-MONOMER.
RETL1328306-WGS:GSTH-112-MONOMER.
UniPathwayUPA00094.

Gene expression databases

GenevestigatorP0A953.

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...

Other

EvolutionaryTraceP0A953.
PROP0A953.

Entry information

Entry nameFABB_ECOLI
AccessionPrimary (citable) accession number: P0A953
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: July 9, 2014
This is version 91 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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