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Entry version 106 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Mannan endo-1,4-beta-mannosidase A

Gene

man1

Organism
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
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

Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and ivory nut mannan, releasing mainly tri- and disaccharides (PubMed:7793911, Ref. 3, Ref. 4, PubMed:8529653). Also has transglycosylation activity. Transglycosylation of two mannotrioses into a mannohexaose is the major transglycosylation route (PubMed:8529653, Ref. 7, PubMed:24950755).6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 '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=0.0015 mg/ml for locust bean gum mannan1 Publication
  2. KM=0.6 mg/ml for locust bean gum mannan1 Publication
  3. KM=0.25 mM for 4-methylumbelliferyl-mannotrioside1 Publication
  4. KM=0.31 mM for mannotetraose1 Publication
  5. KM=0.08 mM for mannopentaose1 Publication
  6. KM=0.05 mM for mannohexaose1 Publication

    pH dependencei

    Optimum pH is 5.0. Stable from pH 2.5 to 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 75 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei196Proton donor/acceptor1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei198Important for transglycosylation activity1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei232SubstrateCombined sources1 Publication1
    Binding sitei274SubstrateCombined sources1 Publication1
    Active sitei303Nucleophile1 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

    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

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    CBM1 Carbohydrate-Binding Module Family 1
    GH5 Glycoside Hydrolase Family 5

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.783 Publications)
    Alternative name(s):
    Beta-mannanase 5A
    Short name:
    Man5A1 Publication
    Beta-mannanase I/II1 Publication
    Short name:
    BMANI
    Short name:
    BMANII
    Endo-beta-1,4-mannanase A
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:man11 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiHypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1344414 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000024376 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unassembled WGS sequence

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi198R → K: Shows an altered product profile, producing mannotriose and mannose from mannotetraose, compared to predominantly mannobiose in the 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 – 19Sequence analysisAdd BLAST19
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044127820 – 271 Publication8
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500432268328 – 437Mannan endo-1,4-beta-mannosidase AAdd BLAST410

    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 bondi53 ↔ 56Combined sources1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi157N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Glycosylationi184N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Disulfide bondi199 ↔ 202Combined sources1 Publication
    Glycosylationi277N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Disulfide bondi292 ↔ 299Combined sources1 Publication
    Disulfide bondi311 ↔ 361Combined sources1 Publication
    Glycosylationi355N-linked (GlcNAc...) asparagineCombined sources1 Publication1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q99036

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    By similarity

    <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

    1437
    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
    Q99036

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q99036

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini400 – 435CBM1PROSITE-ProRule annotationAdd BLAST36

    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>Regioni28 – 376Catalytic1 PublicationAdd BLAST349
    Regioni196 – 198Substrate bindingCombined sources1 Publication3
    Regioni377 – 399Linker1 PublicationAdd BLAST23

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence (Probable). The CBM binds to cellulose but not to mannan, and increases the mannan-hydrolysis of complex substrates (PubMed:12523968).1 Publication1 Publication

    <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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IIG3 Eukaryota
    COG3934 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K19355

    Database of Orthologous Groups

    More...
    OrthoDBi
    1003648at2759

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR035971 CBD_sf
    IPR000254 Cellulose-bd_dom_fun
    IPR001547 Glyco_hydro_5
    IPR017853 Glycoside_hydrolase_SF

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00734 CBM_1, 1 hit
    PF00150 Cellulase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00236 fCBD, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51445 SSF51445, 1 hit
    SSF57180 SSF57180, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00562 CBM1_1, 1 hit
    PS51164 CBM1_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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    Q99036-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MMMLSKSLLS AATAASALAA VLQPVPRASS FVTISGTQFN IDGKVGYFAG
    60 70 80 90 100
    TNCYWCSFLT NHADVDSTFS HISSSGLKVV RVWGFNDVNT QPSPGQIWFQ
    110 120 130 140 150
    KLSATGSTIN TGADGLQTLD YVVQSAEQHN LKLIIPFVNN WSDYGGINAY
    160 170 180 190 200
    VNAFGGNATT WYTNTAAQTQ YRKYVQAVVS RYANSTAIFA WELGNEPRCN
    210 220 230 240 250
    GCSTDVIVQW ATSVSQYVKS LDSNHLVTLG DEGLGLSTGD GAYPYTYGEG
    260 270 280 290 300
    TDFAKNVQIK SLDFGTFHLY PDSWGTNYTW GNGWIQTHAA ACLAAGKPCV
    310 320 330 340 350
    FEEYGAQQNP CTNEAPWQTT SLTTRGMGGD MFWQWGDTFA NGAQSNSDPY
    360 370 380 390 400
    TVWYNSSNWQ CLVKNHVDAI NGGTTTPPPV SSTTTTSSRT SSTPPPPGGS
    410 420 430
    CSPLYGQCGG SGYTGPTCCA QGTCIYSNYW YSQCLNT
    Length:437
    Mass (Da):47,053
    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:i17513DADE12654A7
    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
    L25310 mRNA Translation: AAA34208.1
    KI911141 Genomic DNA Translation: ETS04541.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    ETS04541; ETS04541; M419DRAFT_122377

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    trr:M419DRAFT_122377

    <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
    L25310 mRNA Translation: AAA34208.1
    KI911141 Genomic DNA Translation: ETS04541.1

    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
    1QNOX-ray2.00A28-371[»]
    1QNPX-ray1.50A28-371[»]
    1QNQX-ray1.65A28-371[»]
    1QNRX-ray1.40A28-371[»]
    1QNSX-ray1.50A28-371[»]
    SMRiQ99036
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    CAZyiCBM1 Carbohydrate-Binding Module Family 1
    GH5 Glycoside Hydrolase Family 5

    PTM databases

    iPTMnetiQ99036

    Genome annotation databases

    EnsemblFungiiETS04541; ETS04541; M419DRAFT_122377
    KEGGitrr:M419DRAFT_122377

    Phylogenomic databases

    eggNOGiENOG410IIG3 Eukaryota
    COG3934 LUCA
    KOiK19355
    OrthoDBi1003648at2759

    Miscellaneous databases

    EvolutionaryTraceiQ99036

    Family and domain databases

    InterProiView protein in InterPro
    IPR035971 CBD_sf
    IPR000254 Cellulose-bd_dom_fun
    IPR001547 Glyco_hydro_5
    IPR017853 Glycoside_hydrolase_SF
    PfamiView protein in Pfam
    PF00734 CBM_1, 1 hit
    PF00150 Cellulase, 1 hit
    SMARTiView protein in SMART
    SM00236 fCBD, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit
    SSF57180 SSF57180, 1 hit
    PROSITEiView protein in PROSITE
    PS00562 CBM1_1, 1 hit
    PS51164 CBM1_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 nameiMANA_HYPJR
    <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: Q99036
    Secondary accession number(s): A0A024SIJ3
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2017
    Last sequence update: November 1, 1996
    Last modified: December 11, 2019
    This is version 106 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, Direct protein sequencing

    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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