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Entry version 89 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Avenacosidase 1

Gene

P60A

Organism
Avena sativa (Oat)
Status
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

Beta-glucosidase acting as a preformed defense system. Hydrolyzes the bisdesmosides avenacosides A and B to 26-desgluco-avenacosides exhibiting fungicidal activity. Can use beta-fucoside > beta-glucoside > beta-galactoside > beta-xyloside as substrates, but not alpha-glycosides, beta-thioglucosides and disaccharides.3 Publications

Miscellaneous

Long fibrillar homomultimers are formed by linear stacking of trimeric units. The multimerization of the enzyme promotes formation of a long central channel with narrow openings at the sides. The active sites are localized inside the tunnels, constraining the accessibility of substrates and products.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Inhibited by N-(3-Dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (EDC).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

The activity increases with rising aggregation of the enzyme. kcat is 982000 sec(-1) with avenacosides as substrate. kcat is 3090 sec(-1) with p-nitrophenyl-beta-D-glucopyranoside as substrate. kcat is 290 sec(-1) with genistin as substrate.
  1. KM=2.2 mM for p-nitrophenyl-beta-D-glucopyranoside (with native enzyme)3 Publications
  2. KM=1.57 mM for p-nitrophenyl-beta-D-glucopyranoside (with homomultimeric recombinant enzyme)3 Publications
  3. KM=1.48 mM for p-nitrophenyl-beta-D-glucopyranoside (with heteromultimeric recombinant enzyme)3 Publications
  4. KM=12 µM for avenacosides (with native enzyme)3 Publications
  5. KM=0.4 mM for genistin (with native enzyme)3 Publications

    pH dependencei

    Optimum pH is 6.0.3 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei88SubstrateBy similarity1
    Binding sitei237SubstrateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei238Proton donorBy similarity1
    Active sitei454NucleophileBy similarity1
    Binding sitei505SubstrateBy similarity1

    <p>The <a href="http://www.geneontology.org/">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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">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 functionGlycosidase, Hydrolase
    Biological processPlant defense

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.2.1.186 588

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH1 Glycoside Hydrolase Family 1

    <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="http://www.uniprot.org/help/names_and_taxonomy_section">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:
    Avenacosidase 1 (EC:3.2.1.188)
    Alternative name(s):
    26-desgluco-avenacosidase 1
    Protein As-Glu1
    Protein As-P60
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:P60A
    Synonyms:GLU1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiAvena sativa (Oat)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri4498 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaPoalesPoaceaeBOP cladePooideaePoodaePoeaeAveninaeAvena

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chloroplast, Plastid

    <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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 55Chloroplast3 PublicationsAdd BLAST55
    <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_500014624156 – 574Avenacosidase 1Add BLAST519

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi258 ↔ 264By similarity

    Keywords - PTMi

    Disulfide bond

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in caryopses, coleoptiles, primary leaves, and etiolated and green seedlings, but not in roots.1 Publication

    <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="http://www.uniprot.org/help/interaction_section">'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="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homo- and heteromultimer with P60B in a 1:1 stoichiometry. Aggregates to form the fibrillar stromacentre.

    2 Publications

    GO - Molecular functioni

    <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

    3D structure databases

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

    More...
    SMRi
    Q38786

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni512 – 513Substrate bindingBy similarity2

    <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 glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K20835

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001360 Glyco_hydro_1
    IPR033132 Glyco_hydro_1_N_CS
    IPR017853 Glycoside_hydrolase_SF

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10353 PTHR10353, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00232 Glyco_hydro_1, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00131 GLHYDRLASE1

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51445 SSF51445, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00653 GLYCOSYL_HYDROL_F1_2, 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="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">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="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q38786-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MALLCSALSN STHPSFRSHI GANSENLWHL SADPAQKSKR RCNLTLSSRA
    60 70 80 90 100
    ARISSALESA KQVKPWQVPK RDWFPPEFMF GAASAAYQIE GAWNEGGKGP
    110 120 130 140 150
    SSWDNFCHSH PDRIMDKSNA DVAANSYYMY KEDVRMLKEI GMDSYRFSIS
    160 170 180 190 200
    WPRILPKGTL DGGINHEGIQ YYNDLLDCLI ENGIKPYITL FHWDTPQALA
    210 220 230 240 250
    DEYKDFLDRR IVKDYTDYAT VCFEHFGDKV KNWFTFNEPH SFCGLGYGTG
    260 270 280 290 300
    LHAPGARCSA GMTCVIPEED ALRNPYIVGH NLLLAHAETV DVYNKFYKGD
    310 320 330 340 350
    DGQIGMVLDV MAYEPYGNNF LDQQAQERAI DFHIGWFLEP MVRGDYPFSM
    360 370 380 390 400
    RSLVGDRLPF FTKSEQEKLV SSYDFVGINY YTSRFAKHID ISPEFIPKIN
    410 420 430 440 450
    TDDVYSNPEV NDSNGIPIGP DVGMYFIYSY PKGLKNILLR MKEKYGNPPI
    460 470 480 490 500
    YITENGTADM DGWGNPPMTD PLDDPLRIEY LQQHMTAIKE AIDLGRRTLR
    510 520 530 540 550
    GHFTWSLIDN FEWSLGYLSR FGIVYIDRND GCKRIMKKSA KWLKEFNGAT
    560 570
    KKLNNKILGA SSCCSGVTHG GGTA
    Length:574
    Mass (Da):65,041
    Last modified:November 1, 1996 - 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="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5C6312DCAF251631
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X78433 mRNA Translation: CAA55196.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S43128
    S45723
    S50756

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:CAA55196

    <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="http://www.uniprot.org/help/uniref">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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X78433 mRNA Translation: CAA55196.1
    PIRiS43128
    S45723
    S50756

    3D structure databases

    SMRiQ38786
    ModBaseiSearch...

    Protein family/group databases

    CAZyiGH1 Glycoside Hydrolase Family 1

    Genome annotation databases

    KEGGiag:CAA55196

    Phylogenomic databases

    KOiK20835

    Enzyme and pathway databases

    BRENDAi3.2.1.186 588

    Family and domain databases

    InterProiView protein in InterPro
    IPR001360 Glyco_hydro_1
    IPR033132 Glyco_hydro_1_N_CS
    IPR017853 Glycoside_hydrolase_SF
    PANTHERiPTHR10353 PTHR10353, 1 hit
    PfamiView protein in Pfam
    PF00232 Glyco_hydro_1, 1 hit
    PRINTSiPR00131 GLHYDRLASE1
    SUPFAMiSSF51445 SSF51445, 1 hit
    PROSITEiView protein in PROSITE
    PS00653 GLYCOSYL_HYDROL_F1_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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 nameiAVCO1_AVESA
    <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: Q38786
    <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="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: November 1, 1996
    Last modified: December 11, 2019
    This is version 89 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 programPlant 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
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