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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

Manual assertion based on experiment ini

  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

    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
    Active sitei2945-glutamyl coenzyme A thioester intermediate1 Publication1
    Binding sitei364Coenzyme A; via carbonyl oxygen1 Publication1
    Binding sitei384Coenzyme A1 Publication1
    Binding sitei388Coenzyme A; via amide nitrogen1 Publication1
    Binding sitei408Coenzyme A1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi294E → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi357C → Y: Strongly impaired protein solubility. 1 Publication1
    Mutagenesisi435E → A or Q: Abolishes protein solubility. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004307831 – 505Succinyl-CoA:acetate CoA-transferaseAdd BLAST505

    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

    1505
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi9 – 13Combined sources5
    Helixi17 – 21Combined sources5
    Beta strandi29 – 32Combined sources4
    Helixi43 – 57Combined sources15
    Beta strandi64 – 67Combined sources4
    Turni74 – 76Combined sources3
    Helixi77 – 82Combined sources6
    Beta strandi86 – 91Combined sources6
    Helixi96 – 103Combined sources8
    Beta strandi106 – 109Combined sources4
    Helixi114 – 116Combined sources3
    Helixi117 – 123Combined sources7
    Turni124 – 126Combined sources3
    Beta strandi131 – 139Combined sources9
    Beta strandi145 – 147Combined sources3
    Helixi154 – 160Combined sources7
    Beta strandi162 – 169Combined sources8
    Helixi174 – 176Combined sources3
    Beta strandi179 – 182Combined sources4
    Beta strandi187 – 192Combined sources6
    Beta strandi206 – 210Combined sources5
    Helixi214 – 216Combined sources3
    Beta strandi217 – 223Combined sources7
    Helixi237 – 255Combined sources19
    Beta strandi266 – 268Combined sources3
    Helixi272 – 283Combined sources12
    Beta strandi288 – 296Combined sources9
    Helixi298 – 306Combined sources9
    Beta strandi307 – 317Combined sources11
    Helixi321 – 329Combined sources9
    Helixi331 – 335Combined sources5
    Beta strandi338 – 342Combined sources5
    Helixi343 – 346Combined sources4
    Helixi349 – 355Combined sources7
    Beta strandi358 – 361Combined sources4
    Beta strandi364 – 367Combined sources4
    Beta strandi372 – 377Combined sources6
    Turni378 – 380Combined sources3
    Helixi389 – 395Combined sources7
    Beta strandi396 – 402Combined sources7
    Beta strandi405 – 407Combined sources3
    Turni408 – 411Combined sources4
    Beta strandi412 – 418Combined sources7
    Helixi426 – 428Combined sources3
    Beta strandi431 – 434Combined sources4
    Beta strandi437 – 440Combined sources4
    Helixi446 – 456Combined sources11
    Turni460 – 462Combined sources3
    Helixi463 – 476Combined sources14
    Beta strandi478 – 482Combined sources5
    Turni486 – 490Combined sources5
    Helixi491 – 499Combined sources9

    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[»]
    ProteinModelPortaliB3EY95.
    SMRiB3EY95.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni269 – 273Coenzyme A binding1 Publication5

    Sequence similaritiesi

    Phylogenomic databases

    KOiK18118.

    Family and domain databases

    InterProiIPR026888. AcetylCoA_hyd_C.
    IPR003702. ActCoA_hydro.
    IPR017821. Succinate_CoA_transferase.
    [Graphical view]
    PANTHERiPTHR21432. PTHR21432. 1 hit.
    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 differs from that shown. Reason: Frameshift at position 54.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti357C → Y in AGG68324 (Ref. 3) 1

    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.

    Genome annotation databases

    KEGGiag:ACD85596.

    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[»]
    ProteinModelPortaliB3EY95.
    SMRiB3EY95.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:ACD85596.

    Phylogenomic databases

    KOiK18118.

    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]
    PANTHERiPTHR21432. PTHR21432. 1 hit.
    PfamiPF13336. AcetylCoA_hyd_C. 1 hit.
    PF02550. AcetylCoA_hydro. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03458. YgfH_subfam. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 29 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

    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.