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Entry version 27 (18 Sep 2019)
Sequence version 1 (23 Sep 2008)
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Saccharolobus solfataricus (Sulfolobus solfataricus)
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Has a broad substrate specificity. Hydrolyzes various p-nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids in vitro. Most active against paraoxon, phenyl acetate and p-nitrophenyl caproate (C6), respectively. Has also tributyrinase activity, but shows no hydrolytic activity toward other triacylglycerols including tricaprylin, trimyristin, tripalmitin or triolein in vitro.1 Publication

<p>This subsection of the <a href="">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.1 Publication EC:

<p>This subsection of the <a href="">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Completely inhibited by chemical modifiers that are specific to Cys (HgCl2 and p-chloromercuribenzoic acid), His (diethyl pyrocarbonate) and Ser (diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride). No significant effect with chemical modifiers specific to Lys (pyridoxal 5'-phosphate) and Arg (phenylglyoxal). Not inhibited by inhibitors of A-esterases (paraoxon) or C-esterases (physostigmine/eserine). Activity is also not effected by incubation with 5 mM divalent cations for 30 minutes at 30 degrees Celsius or with 10 mM EDTA for 60 minutes at 75 degrees Celsius.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1) with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl caproate (C6) as substrate. kcat is 410 sec(-1) with p-nitrophenyl caprylate (C8) as substrate. kcat is 341 sec(-1) with p-nitrophenyl caprate (C10) as substrate. kcat is 264 sec(-1) with p-nitrophenyl laurate (C12) as substrate. kcat is 265 sec(-1) with p-nitrophenyl palmitate (C16) as substrate. kcat is 269 sec(-1) with p-nitrophenyl phosphate as substrate. kcat is 597 sec(-1) with paraoxon as substrate. kcat is 342 sec(-1) with methyl paraoxon as substrate.1 Publication
  1. KM=17 µM for phenyl acetate (PA)1 Publication
  2. KM=29 µM for alpha-naphthyl acetate (alpha-NA)1 Publication
  3. KM=224 µM for p-nitrophenyl butyrate (C4)1 Publication
  4. KM=31 µM for p-nitrophenyl caproate (C6)1 Publication
  5. KM=28 µM for p-nitrophenyl caprylate (C8)1 Publication
  6. KM=81 µM for p-nitrophenyl caprate (C10)1 Publication
  7. KM=122 µM for p-nitrophenyl laurate (C12)1 Publication
  8. KM=276 µM for p-nitrophenyl palmitate (C16)1 Publication
  9. KM=234 µM for p-nitrophenyl phosphate1 Publication
  10. KM=5 µM for paraoxon1 Publication
  11. KM=246 µM for methyl paraoxon1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 94 degrees Celsius. Very thermostable, but rapidly inactivated above 94 degrees Celsius. Most of the activity is retained for 5 days at 50 degrees Celsius, and approximately 70% of the activity is retained after 5 days at 70 degrees Celsius. 52% of the activity is still retained after 50 hours at 90 degrees Celsius, but completely inactivated after 5 days at 90 degrees Celsius.1 Publication


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1561 Publication1
    Active sitei2511 Publication1
    Active sitei2811 Publication1

    <p>The <a href="">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • aryldialkylphosphatase activity Source: UniProtKB
    • arylesterase activity Source: UniProtKB

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Serine esterase

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    BRENDAi 6163 6163

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    sulac-q4j9s2 Hormone-sensitive_lipase_like

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Arylesterase1 Publication (EC: Publication)
    Short name:
    A-esterase1 Publication
    Alternative name(s):
    Paraoxonase1 Publication (EC: Publication)
    <p>This subsection of the <a href="">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:are1 Publication
    <p>This subsection of the <a href="">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharolobus solfataricus (Sulfolobus solfataricus)Imported
    <p>This subsection of the <a href="">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri2287 [NCBI]
    <p>This subsection of the <a href="">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSaccharolobus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi105C → S: 3-fold loss of activity compared to wild-type. 1 Publication1
    Mutagenesisi107C → S: 4-fold loss of activity compared to wild-type. 1 Publication1
    Mutagenesisi129C → S: 28-fold loss of activity compared to wild-type. 1 Publication1
    Mutagenesisi156S → A: Nearly loss of activity. 1 Publication1
    Mutagenesisi251D → N: Nearly loss of activity. 1 Publication1
    Mutagenesisi281H → N: 5-fold loss of activity compared to wild-type. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004355651 – 306ArylesteraseAdd BLAST306

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei


    1 Publication

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models


    Database of comparative protein structure models


    Protein Data Bank in Europe - Knowledge Base


    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi82 – 84Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the 'GDXG' lipolytic enzyme family.Curated

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    Gene3Di, 1 hit

    Integrated resource of protein families, domains and functional sites

    View protein in InterPro
    IPR029058 AB_hydrolase
    IPR013094 AB_hydrolase_3

    Pfam protein domain database

    View protein in Pfam
    PF07859 Abhydrolase_3, 1 hit

    Superfamily database of structural and functional annotation

    SSF53474 SSF53474, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="">length</a> and <a href="">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="">Sequence</a> section indicates if the <a href="">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    B5BLW5-1 [UniParc]FASTAAdd to basket
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    260 270 280 290 300

    Mass (Da):34,552
    Last modified:September 23, 2008 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i69DB277CFC26F24B

    <p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 35174.88 Da from positions 1 - 306. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database


    GenBank nucleotide sequence database


    DNA Data Bank of Japan; a nucleotide sequence database

    Links Updated
    FM205057 Genomic DNA Translation: CAR57941.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    Links Updated
    FM205057 Genomic DNA Translation: CAR57941.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe


    Protein Data Bank RCSB


    Protein Data Bank Japan

    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum

    Protein family/group databases

    ESTHERisulac-q4j9s2 Hormone-sensitive_lipase_like

    Enzyme and pathway databases

    BRENDAi3.1.1.2 6163 6163

    Family and domain databases

    Gene3Di3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR013094 AB_hydrolase_3
    PfamiView protein in Pfam
    PF07859 Abhydrolase_3, 1 hit
    SUPFAMiSSF53474 SSF53474, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins


    MobiDB: a database of protein disorder and mobility annotations


    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARE_SACSO
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B5BLW5
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 17, 2016
    Last sequence update: September 23, 2008
    Last modified: September 18, 2019
    This is version 27 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing


    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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