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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)DescriptionActionsGraphical viewLength
    Active sitei20UniRule annotation1
    Active sitei38UniRule annotation1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13726. yccX.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi5C → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001585531 – 92AcylphosphataseAdd BLAST92

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi5 ↔ 49UniRule annotation1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP0AB65.
    PRIDEiP0AB65.

    Interactioni

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    192
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 13Combined sources9
    Turni15 – 18Combined sources4
    Helixi23 – 30Combined sources8
    Beta strandi35 – 38Combined sources4
    Beta strandi40 – 42Combined sources3
    Beta strandi44 – 48Combined sources5
    Helixi52 – 64Combined sources13
    Beta strandi70 – 80Combined sources11

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP0AB65.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini5 – 92Acylphosphatase-likeUniRule annotationAdd BLAST88

    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.
    PhylomeDBiP0AB65.

    Family and domain databases

    HAMAPiMF_01450. Acylphosphatase_entero. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GV1NMR-A1-92[»]
    ProteinModelPortaliP0AB65.
    SMRiP0AB65.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260041. 6 interactors.
    DIPiDIP-11502N.
    IntActiP0AB65. 4 interactors.
    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.
    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. 1 hit.
    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...

    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: November 2, 2016
    This is version 94 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.