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Protein

Acylphosphatase

Gene

acyP

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

An acylphosphate + H2O = a carboxylate + phosphate.

Kineticsi

  1. KM=0.12 mM for benzoylphosphate at 25 degrees Celsius1 Publication

    pH dependencei

    Optimum pH is 5.3 at 25 degrees Celsius.1 Publication

    Temperature dependencei

    Optimum temperature is 98 degrees Celsius. Poorly active at 25 degrees Celsius. Thermostable up to 100 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei20 – 2011 Publication
    Active sitei38 – 3811 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-287-MONOMER.
    BRENDAi3.6.1.7. 5244.
    SABIO-RKP84142.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acylphosphatase (EC:3.6.1.7)
    Alternative name(s):
    Acylphosphate phosphohydrolase
    Gene namesi
    Name:acyP
    Ordered Locus Names:PH0305.1
    OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
    Taxonomic identifieri70601 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000000752 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9191AcylphosphatasePRO_0000158560Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi70601.PH0305a.

    Structurei

    Secondary structure

    1
    91
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1311Combined sources
    Beta strandi15 – 184Combined sources
    Helixi19 – 3012Combined sources
    Beta strandi33 – 386Combined sources
    Beta strandi44 – 518Combined sources
    Helixi52 – 6110Combined sources
    Turni62 – 643Combined sources
    Beta strandi70 – 7910Combined sources
    Beta strandi86 – 894Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V3ZX-ray1.72A/B1-91[»]
    1W2IX-ray1.50A/B1-91[»]
    2W4DX-ray2.40A/B/C/D/E/F2-91[»]
    3TNVX-ray1.60A1-91[»]
    ProteinModelPortaliP84142.
    SMRiP84142. Positions 2-91.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP84142.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9187Acylphosphatase-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the acylphosphatase family.Curated
    Contains 1 acylphosphatase-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiarCOG01674. Archaea.
    COG1254. LUCA.
    OMAiFRQSMKE.

    Family and domain databases

    InterProiIPR020456. Acylphosphatase.
    IPR001792. Acylphosphatase-like_dom.
    IPR017968. Acylphosphatase_CS.
    [Graphical view]
    PfamiPF00708. Acylphosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00112. ACYLPHPHTASE.
    SUPFAMiSSF54975. SSF54975. 1 hit.
    PROSITEiPS00150. ACYLPHOSPHATASE_1. 1 hit.
    PS00151. ACYLPHOSPHATASE_2. 1 hit.
    PS51160. ACYLPHOSPHATASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P84142-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAIVRAHLKI YGRVQGVGFR WSMQREARKL GVNGWVRNLP DGSVEAVLEG
    60 70 80 90
    DEERVEALIG WAHQGPPLAR VTRVEVKWEQ PKGEKGFRIV G
    Length:91
    Mass (Da):10,260
    Last modified:September 13, 2004 - v1
    Checksum:i6DDB6B69DBA17087
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000001 Genomic DNA. No translation available.
    RefSeqiWP_010884399.1. NC_000961.1.

    Genome annotation databases

    GeneIDi1444186.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000001 Genomic DNA. No translation available.
    RefSeqiWP_010884399.1. NC_000961.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V3ZX-ray1.72A/B1-91[»]
    1W2IX-ray1.50A/B1-91[»]
    2W4DX-ray2.40A/B/C/D/E/F2-91[»]
    3TNVX-ray1.60A1-91[»]
    ProteinModelPortaliP84142.
    SMRiP84142. Positions 2-91.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi70601.PH0305a.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi1444186.

    Phylogenomic databases

    eggNOGiarCOG01674. Archaea.
    COG1254. LUCA.
    OMAiFRQSMKE.

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-287-MONOMER.
    BRENDAi3.6.1.7. 5244.
    SABIO-RKP84142.

    Miscellaneous databases

    EvolutionaryTraceiP84142.

    Family and domain databases

    InterProiIPR020456. Acylphosphatase.
    IPR001792. Acylphosphatase-like_dom.
    IPR017968. Acylphosphatase_CS.
    [Graphical view]
    PfamiPF00708. Acylphosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00112. ACYLPHPHTASE.
    SUPFAMiSSF54975. SSF54975. 1 hit.
    PROSITEiPS00150. ACYLPHOSPHATASE_1. 1 hit.
    PS00151. ACYLPHOSPHATASE_2. 1 hit.
    PS51160. ACYLPHOSPHATASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
    2. "Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii."
      Cheung Y.-Y., Allen M.D., Bycroft M., Wong K.-B.
      Acta Crystallogr. D 60:1308-1310(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    3. "Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3."
      Miyazono K.I., Kudo N., Tanokura M.
      Acta Crystallogr. D 60:1135-1136(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
    4. "Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii -- structural insights into enzymatic catalysis, thermostability, and dimerization."
      Cheung Y.-Y., Lam S.Y., Chu W.-K., Allen M.D., Bycroft M., Wong K.-B.
      Biochemistry 44:4601-4611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE.
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

    Entry informationi

    Entry nameiACYP_PYRHO
    AccessioniPrimary (citable) accession number: P84142
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: September 13, 2004
    Last modified: January 20, 2016
    This is version 80 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, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.