Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-ketoacyl-CoA thiolase

Gene

fadA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids.2 Publications

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Kineticsi

  1. KM=96 µM for acetoacetyl-CoA1 Publication
  2. KM=102 µM for CoASH1 Publication

    Pathwayi: fatty acid beta-oxidation

    This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911Acyl-thioester intermediateBy similarity
    Active sitei343 – 3431Proton acceptorBy similarity
    Active sitei373 – 3731Proton acceptorBy similarity

    GO - Molecular functioni

    • acetyl-CoA C-acyltransferase activity Source: UniProtKB

    GO - Biological processi

    • fatty acid beta-oxidation Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:FADA-MONOMER.
    ECOL316407:JW5578-MONOMER.
    MetaCyc:FADA-MONOMER.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-ketoacyl-CoA thiolase (EC:2.3.1.16)
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
    Fatty acid oxidation complex subunit beta
    Gene namesi
    Name:fadA
    Synonyms:oldA
    Ordered Locus Names:b3845, JW5578
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10278. fadA.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3873873-ketoacyl-CoA thiolasePRO_0000206372Add
    BLAST

    Proteomic databases

    EPDiP21151.
    PaxDbiP21151.
    PRIDEiP21151.

    Expressioni

    Inductioni

    Repressed by FadR in the absence of LCFAs (fatty acids of, at least, 12 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs which bind to FadR resulting in its release from the DNA and thus derepression of the transcription.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).1 Publication

    Protein-protein interaction databases

    BioGridi4263456. 162 interactions.
    DIPiDIP-9559N.
    STRINGi511145.b3845.

    Structurei

    3D structure databases

    ProteinModelPortaliP21151.
    SMRiP21151. Positions 1-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CHU. Bacteria.
    COG0183. LUCA.
    HOGENOMiHOG000012239.
    InParanoidiP21151.
    KOiK00632.
    OMAiPQGKEDG.
    OrthoDBiEOG68M4GV.
    PhylomeDBiP21151.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    HAMAPiMF_01620. FadA.
    InterProiIPR012805. FadA.
    IPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    TIGR02445. fadA. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21151-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL
    60 70 80 90 100
    DDIYWGCVQQ TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD
    110 120 130 140 150
    AARMIMTGDA QACLVGGVEH MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT
    160 170 180 190 200
    AEMLARMHGI SREMQDAFAA RSHARAWAAT QSAAFKNEII PTGGHDADGV
    210 220 230 240 250
    LKQFNYDEVI RPETTVEALA TLRPAFDPVN GMVTAGTSSA LSDGAAAMLV
    260 270 280 290 300
    MSESRAHELG LKPRARVRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS
    310 320 330 340 350
    DIGVFEMNEA FAAQILPCIK DLGLIEQIDE KINLNGGAIA LGHPLGCSGA
    360 370 380
    RISTTLLNLM ERKDVQFGLA TMCIGLGQGI ATVFERV
    Length:387
    Mass (Da):40,876
    Last modified:September 27, 2004 - v3
    Checksum:i1A60EF1E6C351704
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371S → T in CAB40810 (PubMed:2204034).Curated
    Sequence conflicti37 – 371S → T in AAA67642 (PubMed:1379743).Curated
    Sequence conflicti119 – 1191E → G in CAB40810 (PubMed:2204034).Curated
    Sequence conflicti371 – 3744TMCI → DGCVS AA sequence (PubMed:2191949).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59368 Genomic DNA. Translation: AAA23751.1.
    M74164 Genomic DNA. Translation: AAA62778.1.
    X52837 Genomic DNA. Translation: CAB40810.1.
    M87049 Genomic DNA. Translation: AAA67642.1.
    U00096 Genomic DNA. Translation: AAT48230.1.
    AP009048 Genomic DNA. Translation: BAE77458.1.
    PIRiF65189. XUEC.
    RefSeqiWP_000438725.1. NZ_LN832404.1.
    YP_026272.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAT48230; AAT48230; b3845.
    BAE77458; BAE77458; BAE77458.
    GeneIDi948324.
    KEGGiecj:JW5578.
    eco:b3845.
    PATRICi32123187. VBIEscCol129921_3959.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59368 Genomic DNA. Translation: AAA23751.1.
    M74164 Genomic DNA. Translation: AAA62778.1.
    X52837 Genomic DNA. Translation: CAB40810.1.
    M87049 Genomic DNA. Translation: AAA67642.1.
    U00096 Genomic DNA. Translation: AAT48230.1.
    AP009048 Genomic DNA. Translation: BAE77458.1.
    PIRiF65189. XUEC.
    RefSeqiWP_000438725.1. NZ_LN832404.1.
    YP_026272.1. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP21151.
    SMRiP21151. Positions 1-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263456. 162 interactions.
    DIPiDIP-9559N.
    STRINGi511145.b3845.

    Proteomic databases

    EPDiP21151.
    PaxDbiP21151.
    PRIDEiP21151.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAT48230; AAT48230; b3845.
    BAE77458; BAE77458; BAE77458.
    GeneIDi948324.
    KEGGiecj:JW5578.
    eco:b3845.
    PATRICi32123187. VBIEscCol129921_3959.

    Organism-specific databases

    EchoBASEiEB0274.
    EcoGeneiEG10278. fadA.

    Phylogenomic databases

    eggNOGiENOG4105CHU. Bacteria.
    COG0183. LUCA.
    HOGENOMiHOG000012239.
    InParanoidiP21151.
    KOiK00632.
    OMAiPQGKEDG.
    OrthoDBiEOG68M4GV.
    PhylomeDBiP21151.

    Enzyme and pathway databases

    UniPathwayiUPA00659.
    BioCyciEcoCyc:FADA-MONOMER.
    ECOL316407:JW5578-MONOMER.
    MetaCyc:FADA-MONOMER.

    Miscellaneous databases

    PROiP21151.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    HAMAPiMF_01620. FadA.
    InterProiIPR012805. FadA.
    IPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    TIGR02445. fadA. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes."
      Dirusso C.C.
      J. Bacteriol. 172:6459-6468(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon."
      Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M.
      J. Biol. Chem. 265:10424-10429(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
      Strain: K12.
    3. "Nucleotide sequence of the fadA and fadB genes from Escherichia coli."
      Nakahigashi K., Inokuchi H.
      Nucleic Acids Res. 18:4937-4937(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. Cited for: SEQUENCE REVISION TO 37.
    7. "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.
    8. "Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli."
      Pramanik A., Pawar S., Antonian E., Schulz H.
      J. Bacteriol. 137:469-473(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    9. "Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli."
      Yang S.Y., Elzinga M.
      J. Biol. Chem. 268:6588-6592(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    10. "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.
    11. "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway."
      Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.
      Mol. Microbiol. 47:793-805(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiFADA_ECOLI
    AccessioniPrimary (citable) accession number: P21151
    Secondary accession number(s): P78130, Q2M8E8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: September 27, 2004
    Last modified: March 16, 2016
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.