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Entry version 81 (18 Sep 2019)
Sequence version 1 (06 Mar 2007)
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Protein

Beta-galactosidase A

Gene

lacA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.1 Publication

Miscellaneous

Mutants of this enzyme have improved transgalactosylation activity and can be used for galacto-oligosaccharides (GOS) production in vitro.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

  • Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.1 Publication EC:3.2.1.23

<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 214.9 s(-1).1 Publication
  1. KM=92.5 mM for lactose1 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 sitei96SubstrateCombined sources1 Publication1
    Binding sitei199SubstrateCombined sources1 Publication1
    <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 sitei200Proton donor1 Publication1
    Active sitei298Nucleophile1 Publication1
    Binding sitei364SubstrateCombined sources1 Publication1

    <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

    • beta-galactosidase activity Source: UniProtKB
    • oligosaccharide binding Source: UniProtKB

    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, Polysaccharide degradation

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH35 Glycoside Hydrolase Family 35

    <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-galactosidase ACurated (EC:3.2.1.231 Publication)
    Short name:
    An-beta-gal1 Publication
    Alternative name(s):
    Lactase A
    <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:lacA
    ORF Names:An01g12150
    <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>OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    <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 identifieri425011 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000006706 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2R

    <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 Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Secreted

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi298E → Q: Loss of hydrolytic activity. 1 Publication1
    Mutagenesisi304Y → A: Nearly complete loss of hydrolytic activity against lactose compared to wild-type due to decreased substrate affinity. 1 Publication1
    Mutagenesisi304Y → F: Over 33% increase of hydrolytic activity against lactose compared to wild-type. No effect on hydrolytic activity compared to wild-type; when associated with H-355 and G-357. 58% reduction in hydrolytic activity compared to wild-type; when associated with H-355, G-357 and F-806. 1 Publication1
    Mutagenesisi355Y → H: No effect on hydrolytic activity compared to wild-type; when associated with F-304 and G-357. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, G-357 and F-806. 1 Publication1
    Mutagenesisi357N → G: No effect on hydrolytic activity compared to wild-type; when associated with F-304 and H-355. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, H-355 and F-806. 1 Publication1
    Mutagenesisi806W → F: 43% loss of hydrolytic activity against lactose compared to wild-type. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, H-355 and G-357. 1 Publication1
    Mutagenesisi806W → S: 90% loss of hydrolytic activity against lactose 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
    <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_500021945819 – 1007Beta-galactosidase ASequence analysisAdd BLAST989

    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>Glycosylationi156N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    <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 bondi205 ↔ 206Combined sources1 Publication
    Disulfide bondi266 ↔ 315Combined sources1 Publication
    Glycosylationi402N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi422N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi478N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi522N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi622N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi739N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi760N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi777N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
    Glycosylationi805N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi914N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    A2QAN3

    PRoteomics IDEntifications database

    More...
    PRIDEi
    A2QAN3

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    A2QAN3

    <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

    11007
    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

    More...
    SMRi
    A2QAN3

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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>Regioni140 – 142Substrate bindingCombined sources1 Publication3

    <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 35 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000181922

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.102.20.10, 1 hit
    2.60.120.260, 2 hits
    2.60.390.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR018954 Betagal_dom2
    IPR037110 Betagal_dom2_sf
    IPR025972 BetaGal_dom3
    IPR036833 BetaGal_dom3_sf
    IPR025300 BetaGal_jelly_roll_dom
    IPR008979 Galactose-bd-like_sf
    IPR031330 Gly_Hdrlase_35_cat
    IPR019801 Glyco_hydro_35_CS
    IPR001944 Glycoside_Hdrlase_35
    IPR017853 Glycoside_hydrolase_SF

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR23421 PTHR23421, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF10435 BetaGal_dom2, 1 hit
    PF13363 BetaGal_dom3, 1 hit
    PF13364 BetaGal_dom4_5, 2 hits
    PF01301 Glyco_hydro_35, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00742 GLHYDRLASE35

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01029 BetaGal_dom2, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF117100 SSF117100, 1 hit
    SSF49785 SSF49785, 2 hits
    SSF51445 SSF51445, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01182 GLYCOSYL_HYDROL_F35, 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.

    A2QAN3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD
    60 70 80 90 100
    KSLFINGERI MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA
    110 120 130 140 150
    LVEGKPGEYR ADGIFDLEPF FDAASEAGIY LLARPGPYIN AESSGGGFPG
    160 170 180 190 200
    WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT IAKYQITNGG PIILYQPENE
    210 220 230 240 250
    YTSGCCGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS GNNAPGTGKG
    260 270 280 290 300
    AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ
    310 320 330 340 350
    GGSYDPWGGP GFAACSELLN NEFERVFYKN DFSFQIAIMN LYMIFGGTNW
    360 370 380 390 400
    GNLGYPNGYT SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP
    410 420 430 440 450
    GNLTTSGYAD TTDLTVTPLL GNSTGSFFVV RHSDYSSEES TSYKLRLPTS
    460 470 480 490 500
    AGSVTIPQLG GTLTLNGRDS KIHVTDYNVS GTNIIYSTAE VFTWKKFADG
    510 520 530 540 550
    KVLVLYGGAG EHHELAISTK SNVTVIEGSE SGISSKQTSS SVVVGWDVST
    560 570 580 590 600
    TRRIIQVGDL KILLLDRNSA YNYWVPQLAT DGTSPGFSTP EKVASSIIVK
    610 620 630 640 650
    AGYLVRTAYL KGSGLYLTAD FNATTSVEVI GVPSTAKNLF INGDKTSHTV
    660 670 680 690 700
    DKNGIWSATV DYNAPDISLP SLKDLDWKYV DTLPEIQSSY DDSLWPAADL
    710 720 730 740 750
    KQTKNTLRSL TTPTSLYSSD YGFHTGYLLY RGHFTATGNE STFAIDTQGG
    760 770 780 790 800
    SAFGSSVWLN GTYLGSWTGL YANSDYNATY NLPQLQAGKT YVITVVIDNM
    810 820 830 840 850
    GLEENWTVGE DLMKTPRGIL NFLLAGRPSS AISWKLTGNL GGEDYEDKVR
    860 870 880 890 900
    GPLNEGGLYA ERQGFHQPEP PSQNWKSSSP LEGLSEAGIG FYSASFDLDL
    910 920 930 940 950
    PKGWDVPLFL NIGNSTTPSP YRVQVYVNGY QYAKYISNIG PQTSFPVPEG
    960 970 980 990 1000
    ILNYRGTNWL AVTLWALDSA GGKLESLELS YTTPVLTALG EVESVDQPKY

    KKRKGAY
    Length:1,007
    Mass (Da):109,712
    Last modified:March 6, 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:iCD1E91854D7A8A0A
    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
    AM269982 Genomic DNA Translation: CAK44114.1

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_001389622.1, XM_001389585.2

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    CAK44114; CAK44114; An01g12150

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    4977988

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ang:ANI_1_1636014

    <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
    AM269982 Genomic DNA Translation: CAK44114.1
    RefSeqiXP_001389622.1, XM_001389585.2

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5IFPX-ray1.71A1-1007[»]
    5IFTX-ray2.45A1-1007[»]
    5IHRX-ray2.40A1-1007[»]
    5JUVX-ray2.27A1-1007[»]
    5MGCX-ray2.30A1-1007[»]
    5MGDX-ray2.15A1-1007[»]
    SMRiA2QAN3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    CAZyiGH35 Glycoside Hydrolase Family 35

    PTM databases

    iPTMnetiA2QAN3

    Proteomic databases

    PaxDbiA2QAN3
    PRIDEiA2QAN3

    Genome annotation databases

    EnsemblFungiiCAK44114; CAK44114; An01g12150
    GeneIDi4977988
    KEGGiang:ANI_1_1636014

    Phylogenomic databases

    HOGENOMiHOG000181922

    Family and domain databases

    Gene3Di2.102.20.10, 1 hit
    2.60.120.260, 2 hits
    2.60.390.10, 1 hit
    InterProiView protein in InterPro
    IPR018954 Betagal_dom2
    IPR037110 Betagal_dom2_sf
    IPR025972 BetaGal_dom3
    IPR036833 BetaGal_dom3_sf
    IPR025300 BetaGal_jelly_roll_dom
    IPR008979 Galactose-bd-like_sf
    IPR031330 Gly_Hdrlase_35_cat
    IPR019801 Glyco_hydro_35_CS
    IPR001944 Glycoside_Hdrlase_35
    IPR017853 Glycoside_hydrolase_SF
    PANTHERiPTHR23421 PTHR23421, 1 hit
    PfamiView protein in Pfam
    PF10435 BetaGal_dom2, 1 hit
    PF13363 BetaGal_dom3, 1 hit
    PF13364 BetaGal_dom4_5, 2 hits
    PF01301 Glyco_hydro_35, 1 hit
    PRINTSiPR00742 GLHYDRLASE35
    SMARTiView protein in SMART
    SM01029 BetaGal_dom2, 1 hit
    SUPFAMiSSF117100 SSF117100, 1 hit
    SSF49785 SSF49785, 2 hits
    SSF51445 SSF51445, 1 hit
    PROSITEiView protein in PROSITE
    PS01182 GLYCOSYL_HYDROL_F35, 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 nameiBGALA_ASPNC
    <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: A2QAN3
    <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: July 13, 2010
    Last sequence update: March 6, 2007
    Last modified: September 18, 2019
    This is version 81 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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