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Protein

Beta-glucosidase

Gene
N/A
Organism
Wickerhamomyces anomalus (Yeast) (Hansenula anomala)
Status
Reviewed-Annotation score:

Annotation score:3 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>
-Protein inferred from homologyi <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

<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

  • Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. EC:3.2.1.21

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei299By 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 processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00696

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH3 Glycoside Hydrolase Family 3

<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:
Beta-glucosidase (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
<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>OrganismiWickerhamomyces anomalus (Yeast) (Hansenula anomala)
<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 identifieri4927 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeWickerhamomyces

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4168

<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 – 20Sequence analysisAdd BLAST20
<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_000001177721 – 825Beta-glucosidaseAdd BLAST805

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>Glycosylationi21N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi97N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi230N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi271N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi328N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi335N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi537N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi550N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi556N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi578N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi667N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi690N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi718N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi733N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi761N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P06835

<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.

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P06835

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P06835

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

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SMRi
P06835

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

<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 3 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.300, 1 hit
3.40.50.1700, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR019800 Glyco_hydro_3_AS
IPR002772 Glyco_hydro_3_C
IPR036881 Glyco_hydro_3_C_sf
IPR001764 Glyco_hydro_3_N
IPR036962 Glyco_hydro_3_N_sf
IPR017853 Glycoside_hydrolase_SF

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00933 Glyco_hydro_3, 1 hit
PF01915 Glyco_hydro_3_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00133 GLHYDRLASE3

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 1 hit
SSF52279 SSF52279, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00775 GLYCOSYL_HYDROL_F3, 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>.<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.

P06835-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLLPLYGLAS FLVLSQAALV NTSAPQASND DPFNHSPSFY PTPQGGRIND
60 70 80 90 100
GKWQAAFYRA RELVDQMSIA EKVNLTTGVG SASGPCSGNT GSVPRLNISS
110 120 130 140 150
ICVQDGPLSV RAADLTDVFP CGMAASSSFN KQLIYDRAVA IGSEFKGKGA
160 170 180 190 200
DAILGPVYGP MGVKAAGGRG WEGHGPDPYL EGVIAYLQTI GIQSQGVVST
210 220 230 240 250
AKHLIGNEQE HFRFAKKDKH AGKIDPGMFN TSSSLSSEID DRAMHEIYLW
260 270 280 290 300
PFAEAVRGGV SSIMCSYNKL NGSHACQNSY LLNYLLKEEL GFQGFVMTDW
310 320 330 340 350
GALYSGIDAA NAGLDMDMPC EAQYFGGNLT TAVLNGTLPQ DRLDDMATRI
360 370 380 390 400
LSALIYSGVH NPDGPNYNAQ TFLTEGHEYF KQQEGDIVVL NKHVDVRSDI
410 420 430 440 450
NRAVALRSAV EGVVLLKNEH ETLPLGREKV KRISILGQAA GDDSKGTSCS
460 470 480 490 500
LRGCGSGAIG TGYGSGAGTF SYFVTPADGI GARAQQEKIS YEFIGDSWNQ
510 520 530 540 550
AAAMDSALYA DAAIEVANSV AGEEIGDVDG NYGDLNNLTL WHNAVPLIKN
560 570 580 590 600
ISSINNNTIV IVTSGQQIDL EPFIDNENVT AVIYSSYLGQ DFGTVLAKVL
610 620 630 640 650
FGDENPSGKL PFTIAKDVND YIPVIEKVDV PDPVDKFTES IYVDYRYFDK
660 670 680 690 700
YNKPVRYEFG YGLSYSNFSL SDIEIQTLQP FSENAEPAAN YSETYQYKQS
710 720 730 740 750
NMDPSEYTVP EGFKELANYT YPYIHDASSI KANSSYDYPE GYSTEQLDGP
760 770 780 790 800
KSLAAGGLGG NHTCGMLVTL SLLKSQIKVL MLVGLHLNCM LDIQIMMNSQ
810 820
HLQCNYVDLK RCFWIKIILK LFLLN
Length:825
Mass (Da):89,561
Last modified:January 1, 1988 - 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:iA43852FF3DE58B74
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
X02903 Genomic DNA Translation: CAA26662.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B23783 GLHQ

<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
X02903 Genomic DNA Translation: CAA26662.1
PIRiB23783 GLHQ

3D structure databases

ProteinModelPortaliP06835
SMRiP06835
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP06835
ChEMBLiCHEMBL4168

Protein family/group databases

CAZyiGH3 Glycoside Hydrolase Family 3

Proteomic databases

PRIDEiP06835

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00696

Family and domain databases

Gene3Di3.20.20.300, 1 hit
3.40.50.1700, 1 hit
InterProiView protein in InterPro
IPR019800 Glyco_hydro_3_AS
IPR002772 Glyco_hydro_3_C
IPR036881 Glyco_hydro_3_C_sf
IPR001764 Glyco_hydro_3_N
IPR036962 Glyco_hydro_3_N_sf
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00933 Glyco_hydro_3, 1 hit
PF01915 Glyco_hydro_3_C, 1 hit
PRINTSiPR00133 GLHYDRLASE3
SUPFAMiSSF51445 SSF51445, 1 hit
SSF52279 SSF52279, 1 hit
PROSITEiView protein in PROSITE
PS00775 GLYCOSYL_HYDROL_F3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiBGLS_WICAO
<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: P06835
<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: January 1, 1988
Last sequence update: January 1, 1988
Last modified: December 5, 2018
This is version 82 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 programFungal 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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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