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Protein

Acetyl-CoA acetyltransferase

Gene

phaA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA (PubMed:4198758). Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation (PubMed:2670936, PubMed:4198758). Also catalyzes the reverse reaction, i.e. the cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB (PubMed:4198758, PubMed:25152395).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The condensation reaction is inhibited by free CoA. The cleavage reaction is characterized by substrate inhibition by acetoacetyl-CoA, which is partially relieved by free CoA.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=390 µM for acetyl-CoA1 Publication

    pH dependencei

    Optimum pH is 7.8 for the condensation reaction and 8.1 for the reverse cleavage reaction.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: poly-(R)-3-hydroxybutanoate biosynthesis

    This protein is involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis, which is part of Biopolymer metabolism.2 Publications
    View all proteins of this organism that are known to be involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis and in Biopolymer metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei88Acyl-thioester intermediate1 Publication1
    Active sitei349Proton acceptorPROSITE-ProRule annotation1 Publication1
    Active sitei379Proton acceptorPROSITE-ProRule annotation1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processPHB biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-13086

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00917

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Acetyl-CoA acetyltransferase (EC:2.3.1.91 Publication)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    Beta-ketothiolase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:phaA1 Publication
    Synonyms:phbA1 Publication
    Ordered Locus Names:H16_A1438
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri381666 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000008210 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi88C → S: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi156H → A: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi219F → A: About 50% loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi219F → Y: 2-fold increase of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi221R → A: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi248S → A: About 40% loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi349H → A: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1
    Mutagenesisi379C → S: Almost complete loss of acetoacetyl-CoA thiolase activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002064181 – 393Acetyl-CoA acetyltransferaseAdd BLAST393

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    381666.H16_A1438

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1393
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P14611

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P14611

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CHU Bacteria
    COG0183 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000012238

    KEGG Orthology (KO)

    More...
    KOi
    K00626

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WDVYNKF

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00751 thiolase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.47.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000429 Ac-CoA_Ac_transf, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53901 SSF53901, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01930 AcCoA-C-Actrans, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P14611-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTDVVIVSAA RTAVGKFGGS LAKIPAPELG AVVIKAALER AGVKPEQVSE
    60 70 80 90 100
    VIMGQVLTAG SGQNPARQAA IKAGLPAMVP AMTINKVCGS GLKAVMLAAN
    110 120 130 140 150
    AIMAGDAEIV VAGGQENMSA APHVLPGSRD GFRMGDAKLV DTMIVDGLWD
    160 170 180 190 200
    VYNQYHMGIT AENVAKEYGI TREAQDEFAV GSQNKAEAAQ KAGKFDEEIV
    210 220 230 240 250
    PVLIPQRKGD PVAFKTDEFV RQGATLDSMS GLKPAFDKAG TVTAANASGL
    260 270 280 290 300
    NDGAAAVVVM SAAKAKELGL TPLATIKSYA NAGVDPKVMG MGPVPASKRA
    310 320 330 340 350
    LSRAEWTPQD LDLMEINEAF AAQALAVHQQ MGWDTSKVNV NGGAIAIGHP
    360 370 380 390
    IGASGCRILV TLLHEMKRRD AKKGLASLCI GGGMGVALAV ERK
    Length:393
    Mass (Da):40,549
    Last modified:April 1, 1990 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i232C1127E20B3961
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    J04987 Genomic DNA Translation: AAA21972.1
    AM260479 Genomic DNA Translation: CAJ92573.1
    J05003 Genomic DNA Translation: AAA21976.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A34340 XXALAE

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_010810132.1, NC_008313.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAJ92573; CAJ92573; H16_A1438

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    reh:H16_A1438

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04987 Genomic DNA Translation: AAA21972.1
    AM260479 Genomic DNA Translation: CAJ92573.1
    J05003 Genomic DNA Translation: AAA21976.1
    PIRiA34340 XXALAE
    RefSeqiWP_010810132.1, NC_008313.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4O99X-ray1.96A/B/C/D2-393[»]
    4O9AX-ray1.52A/B/C/D2-393[»]
    4O9CX-ray2.00A/B/C/D/E/F/G/H1-393[»]
    ProteinModelPortaliP14611
    SMRiP14611
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi381666.H16_A1438

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAJ92573; CAJ92573; H16_A1438
    KEGGireh:H16_A1438

    Phylogenomic databases

    eggNOGiENOG4105CHU Bacteria
    COG0183 LUCA
    HOGENOMiHOG000012238
    KOiK00626
    OMAiWDVYNKF

    Enzyme and pathway databases

    UniPathwayi
    UPA00917

    BioCyciMetaCyc:MONOMER-13086

    Family and domain databases

    CDDicd00751 thiolase, 1 hit
    Gene3Di3.40.47.10, 2 hits
    InterProiView protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N
    PfamiView protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit
    PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
    SUPFAMiSSF53901 SSF53901, 2 hits
    TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
    PROSITEiView protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTHIL_CUPNH
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P14611
    Secondary accession number(s): Q0KBP8
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: December 5, 2018
    This is version 129 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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