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Entry version 36 (08 May 2019)
Sequence version 1 (22 Jul 2008)
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Protein

Succinyl-CoA:acetate CoA-transferase

Gene
N/A
Organism
Acetobacter aceti
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

Utilizes succinyl-CoA to convert toxic acetate to acetyl-CoA and succinate. Required for growth on acetic acid and for resistance to high levels of acetic acid. Has also low activity with acetoacetate as substrate.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

Subject to competitive inhibition by coenzyme A (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

kcat is 280 s(-1) with acetate. kcat is 201 s(-1) with succinyl-CoA. kcat is 75 s(-1) with acetyl-CoA. kcat is 36.5 s(-1) with acetoacetate. kcat is 70.9 s(-1) with succinate.1 Publication
  1. KM=70 mM for acetate1 Publication
  2. KM=22.1 mM for succinyl-CoA1 Publication
  3. KM=22.3 mM for acetyl-CoA1 Publication
  4. KM=0.9 mM for succinate1 Publication
  5. KM=130 mM for acetoacetate1 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: acetyl-CoA biosynthesis

    This protein is involved in the pathway acetyl-CoA biosynthesis, which is part of Metabolic intermediate biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis.

    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 sitei2945-glutamyl coenzyme A thioester intermediate1 Publication1
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei364Coenzyme A; via carbonyl oxygen1 Publication1
    Binding sitei384Coenzyme A1 Publication1
    Binding sitei388Coenzyme A; via amide nitrogen1 Publication1
    Binding sitei408Coenzyme A1 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

    • transferase activity Source: UniProtKB

    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 functionTransferase

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-17982

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.8.3.18 33
    2.8.3.8 33
    6.2.1.5 33

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    B3EY95

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

    More...
    UniPathwayi
    UPA00340

    <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:
    Succinyl-CoA:acetate CoA-transferase (EC:2.8.3.183 Publications)
    Alternative name(s):
    Succinyl-coenzyme A (CoA):acetate CoA-transferase2 Publications
    Short name:
    SCACT1 Publication
    <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>OrganismiAcetobacter acetiImported
    <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 identifieri435 [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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacterAcetobacter subgen. Acetobacter

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells cannot grow on acetate and have lost the resistance to high levels of acetate, a characteristic of wild-type A.aceti.1 Publication

    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>Mutagenesisi294E → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi357C → Y: Strongly impaired protein solubility. 1 Publication1
    Mutagenesisi435E → A or Q: Abolishes protein solubility. 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_00004307831 – 505Succinyl-CoA:acetate CoA-transferaseAdd BLAST505

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expressed at intermediate levels during the first growth phase, when ethanol is metabolized and acetic acid accumulates in the growth medium. Up-regulated during the second growth phase, when acetate is catabolized.1 Publication

    <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

    Homodimer.2 Publications

    <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

    1505
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    4EU3X-ray1.58A/B1-505[»]
    4EU4X-ray2.80A/B1-505[»]
    4EU5X-ray1.74A/B1-505[»]
    4EU6X-ray1.99A/B1-505[»]
    4EU7X-ray1.70A/B1-505[»]
    4EU8X-ray1.81A/B1-505[»]
    4EU9X-ray1.48A/B1-505[»]
    4EUAX-ray2.40A/B1-505[»]
    4EUBX-ray1.97A/B1-505[»]
    4EUCX-ray2.64A/B1-505[»]
    4EUDX-ray1.95A/B1-505[»]
    5DDKX-ray2.13A/B1-505[»]
    5DW4X-ray1.62A/B1-505[»]
    5DW5X-ray1.66A/B1-505[»]
    5DW6X-ray1.55A/B1-505[»]
    5E5HX-ray2.05A/B1-505[»]

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

    More...
    SMRi
    B3EY95

    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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni269 – 273Coenzyme A binding1 Publication5

    <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

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K18118

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.1080.20, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR026888 AcetylCoA_hyd_C
    IPR038460 AcetylCoA_hyd_C_sf
    IPR003702 ActCoA_hydro
    IPR037171 NagB/RpiA_transferase-like
    IPR017821 Succinate_CoA_transferase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13336 AcetylCoA_hyd_C, 1 hit
    PF02550 AcetylCoA_hydro, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF100950 SSF100950, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03458 YgfH_subfam, 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.

    B3EY95-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTERIRNVAL RSKVCPAETA SELIKHGDVV GTSGFTGAGY PKEVPKALAQ
    60 70 80 90 100
    RMEAAHDRGE KYQISLITGA STGPQLDGEL AKANGVYFRS PFNTDATMRN
    110 120 130 140 150
    RINAGETEYF DNHLGQVAGR AVQGNYGKFN IALVEATAIT EDGGIVPTSS
    160 170 180 190 200
    VGNSQTFLNL AEKVIIEVNE WQNPMLEGIH DIWDGNVSGV PTRDIVPIVR
    210 220 230 240 250
    ADQRVGGPVL RVNPDKIAAI VRTNDRDRNA PFAAPDETAK AIAGYLLDFF
    260 270 280 290 300
    GHEVKQNRLP PSLLPLQSGV GNVANAVLEG LKEGPFENLV GYSEVIQDGM
    310 320 330 340 350
    LAMLDSGRMR IASASSFSLS PEAAEEINNR MDFFRSKIIL RQQDVSNSPG
    360 370 380 390 400
    IIRRLGCIAM NGMIEADIYG NVNSTRVMGS KMMNGIGGSG DFARSSYLSI
    410 420 430 440 450
    FLSPSTAKGG KISAIVPMAA HVDHIMQDAQ IFVTEQGLAD LRGLSPVQRA
    460 470 480 490 500
    REIISKCAHP DYRPMLQDYF DRALKNSFGK HTPHLLTEAL SWHQRFIDTG

    TMLPS
    Length:505
    Mass (Da):54,826
    Last modified:July 22, 2008 - 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:iC02A8779588D2510
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence BAA02549 differs from that shown. Reason: Frameshift at position 54.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti357C → Y in AGG68324 (Ref. 3) 1

    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
    D13291 Genomic DNA Translation: BAA02549.1 Frameshift.
    DQ631551 Genomic DNA Translation: ACD85596.1
    JX475924 Genomic DNA Translation: AGG68319.1
    JX475925 Genomic DNA Translation: AGG68324.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I39486

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:ACD85596

    <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
    D13291 Genomic DNA Translation: BAA02549.1 Frameshift.
    DQ631551 Genomic DNA Translation: ACD85596.1
    JX475924 Genomic DNA Translation: AGG68319.1
    JX475925 Genomic DNA Translation: AGG68324.1
    PIRiI39486

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4EU3X-ray1.58A/B1-505[»]
    4EU4X-ray2.80A/B1-505[»]
    4EU5X-ray1.74A/B1-505[»]
    4EU6X-ray1.99A/B1-505[»]
    4EU7X-ray1.70A/B1-505[»]
    4EU8X-ray1.81A/B1-505[»]
    4EU9X-ray1.48A/B1-505[»]
    4EUAX-ray2.40A/B1-505[»]
    4EUBX-ray1.97A/B1-505[»]
    4EUCX-ray2.64A/B1-505[»]
    4EUDX-ray1.95A/B1-505[»]
    5DDKX-ray2.13A/B1-505[»]
    5DW4X-ray1.62A/B1-505[»]
    5DW5X-ray1.66A/B1-505[»]
    5DW6X-ray1.55A/B1-505[»]
    5E5HX-ray2.05A/B1-505[»]
    SMRiB3EY95
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:ACD85596

    Phylogenomic databases

    KOiK18118

    Enzyme and pathway databases

    UniPathwayi
    UPA00340

    BioCyciMetaCyc:MONOMER-17982
    BRENDAi2.8.3.18 33
    2.8.3.8 33
    6.2.1.5 33
    SABIO-RKiB3EY95

    Family and domain databases

    Gene3Di3.40.1080.20, 1 hit
    InterProiView protein in InterPro
    IPR026888 AcetylCoA_hyd_C
    IPR038460 AcetylCoA_hyd_C_sf
    IPR003702 ActCoA_hydro
    IPR037171 NagB/RpiA_transferase-like
    IPR017821 Succinate_CoA_transferase
    PfamiView protein in Pfam
    PF13336 AcetylCoA_hyd_C, 1 hit
    PF02550 AcetylCoA_hydro, 1 hit
    SUPFAMiSSF100950 SSF100950, 2 hits
    TIGRFAMsiTIGR03458 YgfH_subfam, 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 nameiSCACT_ACEAC
    <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: B3EY95
    Secondary accession number(s): M4MDU8, Q43882
    <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: October 29, 2014
    Last sequence update: July 22, 2008
    Last modified: May 8, 2019
    This is version 36 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

    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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