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Reviewed, UniProtKB/Swiss-Prot P0A6R0 (FABH_ECOLI)

Last modified February 9, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-oxoacyl-[acyl-carrier-protein] synthase 3
    EC=2.3.1.180
Alternative name(s):
    3-oxoacyl-[acyl-carrier-protein] synthase III
    Beta-ketoacyl-ACP synthase III
      Short name=KAS III
    EcFabH
Gene names
Name: fabH
Ordered Locus Names: b1091, JW1077
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length317 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. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain. HAMAP MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815

Enzyme regulation

Negatively regulated by acyl-ACP, possibly by binding to either the free enzyme or the acyl-enzyme intermediate. Ref.8

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer. HAMAP MF_01815

Subcellular location

Cytoplasm HAMAP MF_01815.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH. Ref.9

Miscellaneous

Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin and thiolactomycin. HAMAP MF_01815

Sequence similarities

Belongs to the fabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3173173-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_0000110424

Regions

Region245 – 2495ACP-binding HAMAP MF_01815

Sites

Active site1121 HAMAP MF_01815
Active site2441 HAMAP MF_01815
Active site2741 HAMAP MF_01815

Experimental info

Mutagenesis1121C → S: Loss of activity.
Mutagenesis2141K → E or A: Strongly reduces the binding to malonyl-ACP but not that of the substrate. Ref.9
Mutagenesis2441H → A: Loss of activity.
Mutagenesis2491R → E or A: Abolishes the binding to malonyl-ACP but not that of the substrate. Ref.9
Mutagenesis2531A → Y: Abolishes both binding to malonyl-ACP and binding to substrate. Ref.9
Mutagenesis256 – 2572KK → AA: Strongly reduces both binding to malonyl-ACP and binding to substrate.
Mutagenesis256 – 2572KK → EE: Abolishes the binding to malonyl-ACP but not that of the substrate.
Mutagenesis2741N → A: Loss of activity.

Secondary structure

......................................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6R0-1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: BF3192CFF36023D3

FASTA31733,515
        10         20         30         40         50         60 
MYTKIIGTGS YLPEQVRTNA DLEKMVDTSD EWIVTRTGIR ERHIAAPNET VSTMGFEAAT 

        70         80         90        100        110        120 
RAIEMAGIEK DQIGLIVVAT TSATHAFPSA ACQIQSMLGI KGCPAFDVAA ACAGFTYALS 

       130        140        150        160        170        180 
VADQYVKSGA VKYALVVGSD VLARTCDPTD RGTIIIFGDG AGAAVLAASE EPGIISTHLH 

       190        200        210        220        230        240 
ADGSYGELLT LPNADRVNPE NSIHLTMAGN EVFKVAVTEL AHIVDETLAA NNLDRSQLDW 

       250        260        270        280        290        300 
LVPHQANLRI ISATAKKLGM SMDNVVVTLD RHGNTSAASV PCALDEAVRD GRIKPGQLVL 

       310 
LEAFGGGFTW GSALVRF 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12."
Tsay J.-T., Oh W., Larson T.J., Jackowski S., Rock C.O.
J. Biol. Chem. 267:6807-6814(1992) [PubMed: 1551888] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30.
Strain: K12.
[2]"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: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the Escherichia coli K-12 chromosome."
Oh W., Larson T.J.
J. Bacteriol. 174:7873-7874(1992) [PubMed: 1447160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
Strain: K12.
[5]"Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase."
Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J., Stuitje A.R.
J. Bacteriol. 174:2851-2857(1992) [PubMed: 1314802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-317.
[6]"Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli."
Magnuson K., Oh W., Larson T.J., Cronan J.E. Jr.
FEBS Lett. 299:262-266(1992) [PubMed: 1339356] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-317.
Strain: K12.
[7]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-317.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:10996-11000(1996) [PubMed: 8631920] [Abstract]
Cited for: ENZYME REGULATION.
[9]"Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III."
Zhang Y.-M., Rao M.S., Heath R.J., Price A.C., Olson A.J., Rock C.O., White S.W.
J. Biol. Chem. 276:8231-8238(2001) [PubMed: 11078736] [Abstract]
Cited for: DOMAIN, MUTAGENESIS OF LYS-214; ARG-249; ALA-253 AND 256-LYS-LYS-257.
[10]"Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)."
Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H., Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., Brandt M., Daines R.A., Lonsdale J.T.
J. Biol. Chem. 276:30024-30030(2001) [PubMed: 11375394] [Abstract]
Cited for: INHIBITION BY ANTIBIOTICS.
[11]"Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis."
Qiu X., Janson C.A., Konstantinidis A.K., Nwagwu S., Silverman C., Smith W.W., Khandekar S., Lonsdale J., Abdel-Meguid S.S.
J. Biol. Chem. 274:36465-36471(1999) [PubMed: 10593943] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[12]"The 1.8-A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli."
Davies C., Heath R.J., White S.W., Rock C.O.
Structure 8:185-195(2000) [PubMed: 10673437] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[13]"Refined structures of beta-ketoacyl-acyl carrier protein synthase III."
Qiu X., Janson C.A., Smith W.W., Head M., Lonsdale J., Konstantinidis A.K.
J. Mol. Biol. 307:341-356(2001) [PubMed: 11243824] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77744 Genomic DNA. Translation: AAA23749.1.
M96793 Genomic DNA. Translation: AAB59065.1.
U00096 Genomic DNA. Translation: AAC74175.1.
AP009048 Genomic DNA. Translation: BAA35899.2.
M87040 Genomic DNA. Translation: AAA23741.1.
Z11565 Genomic DNA. Translation: CAA77659.1.
PIRA42431.
RefSeqAP_001717.1.
NP_415609.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EBLX-ray1.80A/B1-317[»]
1HN9X-ray2.00A/B1-317[»]
1HNDX-ray1.60A1-317[»]
1HNHX-ray1.90A1-317[»]
1HNJX-ray1.46A1-317[»]
1HNKX-ray1.90A1-317[»]
1MZSX-ray2.10A1-317[»]
2EFTX-ray2.00A/B1-317[»]
2GYOX-ray2.00A/B1-317[»]
3IL9X-ray1.85A/B1-317[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP0A6R0.

2-D gel databases

2DBase-EcoliP0A6R0.

Genome annotation databases

GeneID946003.
GenomeReviewsGene locus JW1077 in contig AP009048_GR.
Gene locus b1091 in contig U00096_GR.
KEGGecj:JW1077.
eco:b1091.

Organism-specific databases

EchoBASEEB0273.
EcoGeneEG10277. fabH.
CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAGGCAGFC.

Enzyme and pathway databases

BioCycEcoCyc:FABH-MONOMER.
ECOL168927:B1091-MONOMER.
MetaCyc:FABH-MONOMER.
BRENDA2.3.1.180. 189382.

Gene expression databases

GenevestigatorP0A6R0.

Family and domain databases

HAMAPMF_01815. FabH.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Other Resources

DrugBankDB01034. Cerulenin.

Entry information

Entry nameFABH_ECOLI
AccessionPrimary (citable) accession number: P0A6R0
Secondary accession number(s): P24249
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents