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Protein

Acylphosphatase

Gene

yccX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

An acylphosphate + H2O = a carboxylate + phosphate.UniRule annotation1 Publication

Kineticsi

  1. KM=0.54 mM for benzoylphosphate1 Publication

    pH dependencei

    Optimum pH is 5.2-6.5.1 Publication

    Temperature dependencei

    Thermostable. Retains 85-90 % of its activity after 3 hours of incubation at 90 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei20 – 201UniRule annotation
    Active sitei38 – 381UniRule annotation

    GO - Molecular functioni

    • acylphosphatase activity Source: EcoCyc

    GO - Biological processi

    • response to heat Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:G6502-MONOMER.
    ECOL316407:JW5131-MONOMER.
    MetaCyc:G6502-MONOMER.
    BRENDAi3.6.1.7. 2026.
    SABIO-RKP0AB65.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AcylphosphataseUniRule annotation (EC:3.6.1.7UniRule annotation)
    Alternative name(s):
    Acylphosphate phosphohydrolaseUniRule annotation
    Gene namesi
    Name:yccXUniRule annotation
    Ordered Locus Names:b0968, JW5131
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13726. yccX.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51C → A: No change in secondary structure. Nearly identical enzymatic properties. Loss of activity in 8.0 M urea. Reduced thermodynamic activity. Inactivated after 3 hours of incubation at 90 degrees Celsius. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9292AcylphosphatasePRO_0000158553Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi5 ↔ 49UniRule annotation1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP0AB65.
    PRIDEiP0AB65.

    Interactioni

    Protein-protein interaction databases

    BioGridi4260041. 6 interactions.
    DIPiDIP-11502N.
    IntActiP0AB65. 4 interactions.
    STRINGi511145.b0968.

    Structurei

    Secondary structure

    1
    92
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139Combined sources
    Turni15 – 184Combined sources
    Helixi23 – 308Combined sources
    Beta strandi35 – 384Combined sources
    Beta strandi40 – 423Combined sources
    Beta strandi44 – 485Combined sources
    Helixi52 – 6413Combined sources
    Beta strandi70 – 8011Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GV1NMR-A1-92[»]
    ProteinModelPortaliP0AB65.
    SMRiP0AB65. Positions 1-92.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB65.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9288Acylphosphatase-likeUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the acylphosphatase family.UniRule annotation
    Contains 1 acylphosphatase-like domain.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105VSY. Bacteria.
    COG1254. LUCA.
    HOGENOMiHOG000292686.
    InParanoidiP0AB65.
    KOiK01512.
    OMAiMIKSCHT.
    OrthoDBiEOG6ND0QX.
    PhylomeDBiP0AB65.

    Family and domain databases

    HAMAPiMF_01450. Acylphosphatase_entero.
    InterProiIPR020456. Acylphosphatase.
    IPR001792. Acylphosphatase-like_dom.
    IPR028627. Acylphosphatase_bac.
    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.

    P0AB65-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKVCIIAWV YGRVQGVGFR YTTQYEAKRL GLTGYAKNLD DGSVEVVACG
    60 70 80 90
    EEGQVEKLMQ WLKSGGPRSA RVERVLSEPH HPSGELTDFR IR
    Length:92
    Mass (Da):10,300
    Last modified:November 8, 2005 - v1
    Checksum:iC39D3D145598D873
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74054.1.
    AP009048 Genomic DNA. Translation: BAA35733.2.
    PIRiG64837.
    RefSeqiNP_415488.1. NC_000913.3.
    WP_000048252.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74054; AAC74054; b0968.
    BAA35733; BAA35733; BAA35733.
    GeneIDi945304.
    KEGGiecj:JW5131.
    eco:b0968.
    PATRICi32117157. VBIEscCol129921_1003.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74054.1.
    AP009048 Genomic DNA. Translation: BAA35733.2.
    PIRiG64837.
    RefSeqiNP_415488.1. NC_000913.3.
    WP_000048252.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GV1NMR-A1-92[»]
    ProteinModelPortaliP0AB65.
    SMRiP0AB65. Positions 1-92.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260041. 6 interactions.
    DIPiDIP-11502N.
    IntActiP0AB65. 4 interactions.
    STRINGi511145.b0968.

    Proteomic databases

    PaxDbiP0AB65.
    PRIDEiP0AB65.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74054; AAC74054; b0968.
    BAA35733; BAA35733; BAA35733.
    GeneIDi945304.
    KEGGiecj:JW5131.
    eco:b0968.
    PATRICi32117157. VBIEscCol129921_1003.

    Organism-specific databases

    EchoBASEiEB3490.
    EcoGeneiEG13726. yccX.

    Phylogenomic databases

    eggNOGiENOG4105VSY. Bacteria.
    COG1254. LUCA.
    HOGENOMiHOG000292686.
    InParanoidiP0AB65.
    KOiK01512.
    OMAiMIKSCHT.
    OrthoDBiEOG6ND0QX.
    PhylomeDBiP0AB65.

    Enzyme and pathway databases

    BioCyciEcoCyc:G6502-MONOMER.
    ECOL316407:JW5131-MONOMER.
    MetaCyc:G6502-MONOMER.
    BRENDAi3.6.1.7. 2026.
    SABIO-RKP0AB65.

    Miscellaneous databases

    EvolutionaryTraceiP0AB65.
    PROiP0AB65.

    Family and domain databases

    HAMAPiMF_01450. Acylphosphatase_entero.
    InterProiIPR020456. Acylphosphatase.
    IPR001792. Acylphosphatase-like_dom.
    IPR028627. Acylphosphatase_bac.
    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: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli."
      Ramazzotti M., Parrini C., Stefani M., Manao G., Degl'Innocenti D.
      FEBS Lett. 580:6763-6768(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BOND, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-5.
      Strain: K12 / DH5-alpha.
    5. "NMR solution structure of the acylphosphatase from Escherichia coli."
      Pagano K., Ramazzotti M., Viglino P., Esposito G., Degl'Innocenti D., Taddei N., Corazza A.
      J. Biomol. NMR 36:199-204(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiACYP_ECOLI
    AccessioniPrimary (citable) accession number: P0AB65
    Secondary accession number(s): P75877, Q9R7Q1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: January 20, 2016
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has a considerably reduced catalytic efficiency compared to other mesophilic acylphosphatases. Shows a considerable resistance against urea denaturation since the full enzymatic activity is maintained in the presence of urea concentrations approaching 6.0 M and that only a slight decreae of 10-15 % was observed with higher urea concentrations.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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.