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Entry version 41 (11 Dec 2019)
Sequence version 1 (03 Apr 2007)
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Protein

Isoflavonoid 7-O-beta-apiosyl-glucoside beta-glycosidase

Gene
N/A
Organism
Dalbergia nigrescens (Thai blackwood)
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

Hydrolyzes dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside and dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside. Also has activity towards pNP-beta-D-fucoside and pNP-beta-D-glucoside, but not pNP-beta-cellobioside.1 Publication

<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

Not inhibited by iron, calcium, mercury, manganese, zinc or EDTA.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

  1. KM=14.7 mM for pNP-beta-D-glucoside1 Publication
  2. KM=1.8 mM for pNP-beta-D-fucoside1 Publication
  3. KM=0.5 mM for dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside1 Publication
  4. KM=0.7 mM for dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside1 Publication
  5. KM=0.11 mM for daidzin1 Publication
  6. KM=0.09 mM for genistin1 Publication

    pH dependencei

    Optimum pH is 5.0-6.0. Half maximum activity is seen at pH 3.5 and 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius.1 Publication

    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 sitei59SubstrateBy similarity1
    Binding sitei159SubstrateBy similarity1
    Binding sitei204SubstrateBy 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 sitei205Proton donorBy similarity1
    Binding sitei348SubstrateBy similarity1
    Active sitei419NucleophileBy similarity1
    Binding sitei468SubstrateBy 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

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-13779

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.2.1.161 8018

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    A3RF67

    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:
    Isoflavonoid 7-O-beta-apiosyl-glucoside beta-glycosidase1 Publication (EC:3.2.1.161)
    Alternative name(s):
    Beta-glycosidaseImported
    <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>OrganismiDalbergia nigrescens (Thai blackwood)
    <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 identifieri298683 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladedalbergioids sensu latoDalbergieaeDalbergia cladeDalbergia

    <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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 311 PublicationAdd BLAST31
    <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_000039861532 – 547Isoflavonoid 7-O-beta-apiosyl-glucoside beta-glycosidase1 PublicationAdd BLAST516

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi72N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi132N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi175N-linked (GlcNAc...) asparagineSequence analysis1
    <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 bondi224 ↔ 232By similarity
    Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi490N-linked (GlcNAc...) asparagineSequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    <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

    Homotetramer.

    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

    3D structure databases

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

    More...
    SMRi
    A3RF67

    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>Regioni475 – 476Substrate 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.Sequence analysis

    Keywords - Domaini

    Signal

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001360 Glyco_hydro_1
    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

    <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.

    A3RF67-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MHAMTFKAIL LLGLLALVST SASIAFAKEV RATITEVPPF NRNSFPSDFI
    60 70 80 90 100
    FGTAASSYQY EGEGRVPSIW DNFTHQYPEK IADGSNGDVA VDQFHHYKED
    110 120 130 140 150
    VAIMKYMNLD AYRLSISWPR ILPTGRASGG INSTGVDYYN RLINELLAND
    160 170 180 190 200
    ITPFVTIFHW DLPQALEDEY GGFLNHTIVN DFRDYADLCF NLFGDRVKHW
    210 220 230 240 250
    ITVNEPSIFT MNGYAYGIFA PGRCSPSYNP TCTGGDAGTE PDLVAHNLIL
    260 270 280 290 300
    SHAATVQVYK KKYQEHQNGI IGISLQIIWA VPLSNSTSDQ KAAQRYLDFT
    310 320 330 340 350
    GGWFLDPLTA GQYPESMQYL VGDRLPKFTT DEAKLVKGSF DFVGINYYTS
    360 370 380 390 400
    SYLTSSDAST CCPPSYLTDS QVTFSSQRNG VFIGPVTPSG WMCIYPKGLR
    410 420 430 440 450
    DLLLYIKEKY NNPLVYITEN GMDELDDPSQ SLEESLIDTY RIDSYYRHLF
    460 470 480 490 500
    YVRSAIGSGA NVKGFFAWSL LDNFEWNEGF TSRFGLNFVN YTTLTRYHKL
    510 520 530 540
    SATWFKYFLA RDQEIAKLDI SAPKARWSSS TMIKEEKRKP KWAIQAF
    Length:547
    Mass (Da):61,859
    Last modified:April 3, 2007 - 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:i03F4AAA6D54EB8F5
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti146L → T AA sequence (PubMed:16098548).Curated1
    Sequence conflicti150D → G AA sequence (PubMed:16098548).Curated1

    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
    EF392846 mRNA Translation: ABN70849.1

    <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="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
    EF392846 mRNA Translation: ABN70849.1

    3D structure databases

    SMRiA3RF67
    ModBaseiSearch...

    Protein family/group databases

    CAZyiGH1 Glycoside Hydrolase Family 1

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13779
    BRENDAi3.2.1.161 8018
    SABIO-RKiA3RF67

    Family and domain databases

    InterProiView protein in InterPro
    IPR001360 Glyco_hydro_1
    IPR017853 Glycoside_hydrolase_SF
    PANTHERiPTHR10353 PTHR10353, 1 hit
    PfamiView protein in Pfam
    PF00232 Glyco_hydro_1, 1 hit
    PRINTSiPR00131 GLHYDRLASE1
    SUPFAMiSSF51445 SSF51445, 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 nameiBAGBG_DALNI
    <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: A3RF67
    <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: October 5, 2010
    Last sequence update: April 3, 2007
    Last modified: December 11, 2019
    This is version 41 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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