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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-Experimental evidence at protein leveli

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

Catalytic activityi

Succinyl-CoA + acetate = acetyl-CoA + succinate.3 Publications

Enzyme regulationi

Subject to competitive inhibition by coenzyme A (CoA).1 Publication

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 acetate.1 Publication
  2. KM=22.1 mM for succinyl-CoA.1 Publication
  3. KM=22.3 mM for acetyl-CoA.1 Publication
  4. KM=0.9 mM for succinate.1 Publication
  5. KM=130 mM for acetoacetate.1 Publication

    Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei294 – 29415-glutamyl coenzyme A thioester intermediate1 Publication
    Binding sitei364 – 3641Coenzyme A; via carbonyl oxygen1 Publication
    Binding sitei384 – 3841Coenzyme A1 Publication
    Binding sitei388 – 3881Coenzyme A; via amide nitrogen1 Publication
    Binding sitei408 – 4081Coenzyme A1 Publication

    GO - Molecular functioni

    • transferase activity Source: UniProtKB

    GO - Biological processi

    • acetate catabolic process Source: UniProtKB
    • acetyl-CoA biosynthetic process from acetate Source: UniProtKB
    • succinyl-CoA catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17982.
    BRENDAi2.8.3.18. 33.
    2.8.3.8. 33.
    6.2.1.5. 33.
    UniPathwayiUPA00340.

    Names & Taxonomyi

    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
    OrganismiAcetobacter acetiImported
    Taxonomic identifieri435 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacterAcetobacter subgen. Acetobacter

    Pathology & Biotechi

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi294 – 2941E → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi357 – 3571C → Y: Strongly impaired protein solubility. 1 Publication
    Mutagenesisi435 – 4351E → A or Q: Abolishes protein solubility. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505Succinyl-CoA:acetate CoA-transferasePRO_0000430783Add
    BLAST

    Expressioni

    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

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 135Combined sources
    Helixi17 – 215Combined sources
    Beta strandi29 – 324Combined sources
    Helixi43 – 5715Combined sources
    Beta strandi64 – 674Combined sources
    Turni74 – 763Combined sources
    Helixi77 – 826Combined sources
    Beta strandi86 – 916Combined sources
    Helixi96 – 1038Combined sources
    Beta strandi106 – 1094Combined sources
    Helixi114 – 1163Combined sources
    Helixi117 – 1237Combined sources
    Turni124 – 1263Combined sources
    Beta strandi131 – 1399Combined sources
    Beta strandi145 – 1473Combined sources
    Helixi154 – 1607Combined sources
    Beta strandi162 – 1698Combined sources
    Helixi174 – 1763Combined sources
    Beta strandi179 – 1824Combined sources
    Beta strandi187 – 1926Combined sources
    Beta strandi206 – 2105Combined sources
    Helixi214 – 2163Combined sources
    Beta strandi217 – 2237Combined sources
    Helixi237 – 25519Combined sources
    Beta strandi266 – 2683Combined sources
    Helixi272 – 28312Combined sources
    Beta strandi288 – 2969Combined sources
    Helixi298 – 3069Combined sources
    Beta strandi307 – 31711Combined sources
    Helixi321 – 3299Combined sources
    Helixi331 – 3355Combined sources
    Beta strandi338 – 3425Combined sources
    Helixi343 – 3464Combined sources
    Helixi349 – 3557Combined sources
    Beta strandi358 – 3614Combined sources
    Beta strandi364 – 3674Combined sources
    Beta strandi372 – 3776Combined sources
    Turni378 – 3803Combined sources
    Helixi389 – 3957Combined sources
    Beta strandi396 – 4027Combined sources
    Beta strandi405 – 4073Combined sources
    Turni408 – 4114Combined sources
    Beta strandi412 – 4187Combined sources
    Helixi426 – 4283Combined sources
    Beta strandi431 – 4344Combined sources
    Beta strandi437 – 4404Combined sources
    Helixi446 – 45611Combined sources
    Turni460 – 4623Combined sources
    Helixi463 – 47614Combined sources
    Beta strandi478 – 4825Combined sources
    Turni486 – 4905Combined sources
    Helixi491 – 4999Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    4FACX-ray2.05A/B1-505[»]
    ProteinModelPortaliB3EY95.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 2735Coenzyme A binding1 Publication

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR026888. AcetylCoA_hyd_C.
    IPR003702. ActCoA_hydro.
    IPR017821. Succinate_CoA_transferase.
    [Graphical view]
    PfamiPF13336. AcetylCoA_hyd_C. 1 hit.
    PF02550. AcetylCoA_hydro. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03458. YgfH_subfam. 1 hit.

    Sequencei

    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
    Checksum:iC02A8779588D2510
    GO

    Sequence cautioni

    The sequence BAA02549.1 differs from that shown. Reason: Frameshift at position 54. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti357 – 3571C → Y in AGG68324 (Ref. 3)

    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.

    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
    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[»]
    4FACX-ray2.05A/B1-505[»]
    ProteinModelPortaliB3EY95.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00340.
    BioCyciMetaCyc:MONOMER-17982.
    BRENDAi2.8.3.18. 33.
    2.8.3.8. 33.
    6.2.1.5. 33.

    Family and domain databases

    InterProiIPR026888. AcetylCoA_hyd_C.
    IPR003702. ActCoA_hydro.
    IPR017821. Succinate_CoA_transferase.
    [Graphical view]
    PfamiPF13336. AcetylCoA_hyd_C. 1 hit.
    PF02550. AcetylCoA_hydro. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03458. YgfH_subfam. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "The aarC gene responsible for acetic acid assimilation confers acetic acid resistance on Acetobacter aceti."
      Fukaya M., Takemura H., Tayama K., Okumura H., Kawamura Y., Horinouchi S., Beppu T.
      J. Ferment. Bioeng. 76:270-275(1993)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION.
      Strain: 1023Imported.
    2. "A specialized citric acid cycle requiring succinyl-coenzyme A (CoA):acetate CoA-transferase (AarC) confers acetic acid resistance on the acidophile Acetobacter aceti."
      Mullins E.A., Francois J.A., Kappock T.J.
      J. Bacteriol. 190:4933-4940(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: 10231 Publication.
    3. "Functional analysis of the acetic acid resistance (aar) gene cluster in Acetobacter aceti strain 1023."
      Mullins E.A., Kappock T.J.
      Acetic Acid Bacteria 2:E3-E3(2013)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-357, PATHWAY, INDUCTION.
      Strain: 10231 Publication.
    4. "Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases."
      Mullins E.A., Kappock T.J.
      Biochemistry 51:8422-8434(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH COENZYME A AND ACETATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF GLU-435.

    Entry informationi

    Entry nameiSCACT_ACEAC
    AccessioniPrimary (citable) accession number: B3EY95
    Secondary accession number(s): M4MDU8, Q43882
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: July 22, 2008
    Last modified: May 27, 2015
    This is version 24 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

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

    External Data

    Dasty 3

    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 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.