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

Acetate--CoA ligase [ADP-forming] I subunit beta

Gene

acdBI

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as isobutyryl-CoA, propionyl-CoA and butyryl-CoA, but not indoleacetyl-CoA, phenylacetyl-CoA or succinyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-chain amino acids via branched-chain-acyl-CoA esters.3 Publications

Catalytic activityi

ATP + acetate + CoA = ADP + phosphate + acetyl-CoA.3 Publications

Enzyme regulationi

Activity is dependent on magnesium.1 Publication

Kineticsi

kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec(-1) for CoA. kcat is 65 sec(-1) for acetate. kcat is 55 sec(-1) for isobutyrate.1 Publication

  1. KM=150 µM for ADP (at 80 degrees Celsius)1 Publication
  2. KM=60 µM for ADP (at 55 degrees Celsius)1 Publication
  3. KM=132 µM for GDP (at 80 degrees Celsius)1 Publication
  4. KM=396 µM for phosphate (at 80 degrees Celsius)1 Publication
  5. KM=200 µM for phosphate (at 55 degrees Celsius)1 Publication
  6. KM=25 µM for acetyl-CoA (at 80 degrees Celsius)1 Publication
  7. KM=17 µM for acetyl-CoA (at 55 degrees Celsius)1 Publication
  8. KM=29 µM for isobutyryl-CoA (at 80 degrees Celsius)1 Publication
  9. KM=477 µM for ATP (at 80 degrees Celsius)1 Publication
  10. KM=80 µM for ATP (at 55 degrees Celsius)1 Publication
  11. KM=430 µM for GTP (at 80 degrees Celsius)1 Publication
  12. KM=18 µM for CoA (at 80 degrees Celsius)1 Publication
  13. KM=30 µM for CoA (at 55 degrees Celsius)1 Publication
  14. KM=1100 µM for acetate (at 80 degrees Celsius)1 Publication
  15. KM=660 µM for acetate (at 55 degrees Celsius)1 Publication
  16. KM=457 µM for isobutyrate (at 80 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.0 (at 80 degrees Celsius) (PubMed:8830684). Optimum pH is 7.0 (at 55 degrees Celsius) (PubMed:9119024).2 Publications

    Temperature dependencei

    Optimum temperature is above 90 degrees Celsius.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi53 – 6412ATPPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11823.
    BRENDAi6.2.1.13. 5243.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetate--CoA ligase [ADP-forming] I subunit betaCurated (EC:6.2.1.133 Publications)
    Alternative name(s):
    ADP-forming acetyl coenzyme A synthetase I subunit betaCurated
    Short name:
    ACS I subunit betaCurated
    Gene namesi
    Name:acdBI1 Publication
    Ordered Locus Names:PF1787Imported
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000001013 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 232232Acetate--CoA ligase [ADP-forming] I subunit betaPRO_0000430521Add
    BLAST

    Proteomic databases

    PRIDEiE7FHP1.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta subunits.3 Publications

    Protein-protein interaction databases

    STRINGi186497.PF1787.

    Structurei

    3D structure databases

    ProteinModelPortaliE7FHP1.
    SMRiE7FHP1. Positions 5-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 6337ATP-graspPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiarCOG01340. Archaea.
    COG1042. LUCA.
    HOGENOMiHOG000132014.
    KOiK01905.
    OMAiVIVGMIR.

    Family and domain databases

    Gene3Di3.30.470.20. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013816. ATP_grasp_subdomain_2.
    [Graphical view]
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E7FHP1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDRVAKAREI IEKAKAENRP LVEPEAKEIL KLYGIPVPEF KVARNEEEAV
    60 70 80 90 100
    KFSGEIGYPV VMKIVSPQII HKSDAGGVKI NIKNDEEARE AFRTIMQNAR
    110 120 130 140 150
    NYKPDADLWG VIIYRMLPLG REVIVGMIRD PQFGPAVMFG LGGIFVEILK
    160 170 180 190 200
    DVSFRVAPIT KEDALEMIRE IKAYPILAGA RGEKPVNIEA LADIIVKVGE
    210 220 230
    LALELPEIKE IDINPIFAYE DSAIAVDARM IL
    Length:232
    Mass (Da):25,878
    Last modified:March 8, 2011 - v1
    Checksum:i1C00A9AFD2A121D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201P → R AA sequence (PubMed:9119024).Curated
    Sequence conflicti23 – 231E → Q AA sequence (PubMed:8830684).Curated
    Sequence conflicti25 – 251E → A AA sequence (PubMed:8830684).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ240062 Genomic DNA. Translation: CAB46517.1.
    AE009950 Genomic DNA. Translation: AAL81911.1.
    PIRiT48662.
    RefSeqiWP_011012928.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL81911; AAL81911; PF1787.
    GeneIDi1469666.
    KEGGipfu:PF1787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ240062 Genomic DNA. Translation: CAB46517.1.
    AE009950 Genomic DNA. Translation: AAL81911.1.
    PIRiT48662.
    RefSeqiWP_011012928.1. NC_003413.1.

    3D structure databases

    ProteinModelPortaliE7FHP1.
    SMRiE7FHP1. Positions 5-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF1787.

    Proteomic databases

    PRIDEiE7FHP1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL81911; AAL81911; PF1787.
    GeneIDi1469666.
    KEGGipfu:PF1787.

    Phylogenomic databases

    eggNOGiarCOG01340. Archaea.
    COG1042. LUCA.
    HOGENOMiHOG000132014.
    KOiK01905.
    OMAiVIVGMIR.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11823.
    BRENDAi6.2.1.13. 5243.

    Family and domain databases

    Gene3Di3.30.470.20. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013816. ATP_grasp_subdomain_2.
    [Graphical view]
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits."
      Musfeldt M., Selig M., Schonheit P.
      J. Bacteriol. 181:5885-5888(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GENE NAME.
    2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus."
      Mai X., Adams M.W.
      J. Bacteriol. 178:5897-5903(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-27, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    4. "Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus."
      Glasemacher J., Bock A.K., Schmid R., Schoenheit P.
      Eur. J. Biochem. 244:561-567(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-24, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

    Entry informationi

    Entry nameiACDB1_PYRFU
    AccessioniPrimary (citable) accession number: E7FHP1
    Secondary accession number(s): Q7LWX9, Q9Y8L0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: March 8, 2011
    Last modified: November 11, 2015
    This is version 31 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 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.