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Protein

Mannan endo-1,4-beta-mannosidase

Gene

manA

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
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

Catalyzes the endo hydrolysis of beta-1,4-linked mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall (PubMed:11382747). Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides (PubMed:7848261) (PubMed:8973192). It displays tight specificity for mannose at both the -2 and the -1 subsites (PubMed:19441796). Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan (PubMed:11064195).5 Publications

<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 ‘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 14.7 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMed:8973192). Kcat is 20 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMed:11382747). Kcat is 1759 sec(-1) for mannanase activity with carob galactomannan as substrate (PubMed:8973192). Kcat is 2904 sec(-1) for mannanase activity with carob galactomannan as substrate (PubMed:11382747). Kcat is 3861 sec(-1) for mannanase activity with mannotetraose as substrate (PubMed:8973192). Kcat is 280000 min(-1) for mannanase activity with galactomannan as substrate (PubMed:19441796). Kcat is 400000 min(-1) for mannanase activity with glucomannan as substrate (PubMed:19441796).3 Publications
  1. KM=0.9 mg/ml for carob galactomannan1 Publication
  2. KM=2.8 mg/ml for glucomannan1 Publication
  3. KM=3.2 mg/ml for galactomannan1 Publication
  4. KM=9.3 µM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)1 Publication
  5. KM=12.3 µM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)1 Publication

    pH dependencei

    Optimum pH is about 7.0.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei121Substrate2 Publications1
    Binding sitei143Substrate3 Publications1
    Binding sitei162Substrate1 Publication1 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>Sitei211Plays an important role in maintaining the position of the catalytic nucleophile1 Publication1 Publication1
    <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 sitei212Proton donor4 Publications1
    Binding sitei217Substrate1 Publication1
    Binding sitei285Substrate2 Publications1
    Active sitei320Nucleophile2 Publications1
    Binding sitei377Substrate3 Publications1

    <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

    • mannan endo-1,4-beta-mannosidase activity 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

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    CJAP498211:G1GB3-2766-MONOMER

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH26 Glycoside Hydrolase Family 26

    <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:
    Mannan endo-1,4-beta-mannosidase1 Publication (EC:3.2.1.784 Publications)
    Alternative name(s):
    Mannanase 26A1 Publication
    Short name:
    Man26A1 Publication
    Mannanase A1 Publication
    Short name:
    ManA1 Publication
    <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:manA1 Publication
    Synonyms:man26A
    Ordered Locus Names:CJA_2770
    <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>OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    <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 identifieri498211 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
    <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
    • UP000001036 <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

    <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>Mutagenesisi121E → A: Strong decrease of mannanase activity against both oligosaccharides and polysaccharides. 1 Publication1
    Mutagenesisi143H → A: Very low mannanase activity against both mannans and mannooligosaccharides. 1 Publication1
    Mutagenesisi156W → A: Similar to the wild-type. 1 Publication1
    Mutagenesisi162W → A: The mannanase activity is 95, 70, and 30-fold less active than the wild-type against mannotriose, mannotetraose and mannohexaose, respectively. 1 Publication1
    Mutagenesisi211H → A: Causes a 100- and 700-fold decrease in mannanase activity against carob galactomannans and mannotetraose, respectively, but only a 6-fold reduction in mannanase activity against 2,4-DNPM. 1 Publication1
    Mutagenesisi212E → A: Causes a dramatic decrease in the catalytic efficiency against carob galactomannan, azo-carob galactomannan, mannotetraose and 2,4-DNPM. 2 Publications1
    Mutagenesisi212E → D: 10-fold decrease of the catalytic efficiency against 2,4-DNPM. 1 Publication1
    Mutagenesisi217W → A: Lack of mannanase activity against both mannotriose and mannotetraose. 1 Publication1
    Mutagenesisi278D → A: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
    Mutagenesisi278D → E: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
    Mutagenesisi283D → A: Retains significant activity against mannotetraose and azo-carob galactomannan. Lack of activity against all substrates; when associated with A-320. 2 Publications1
    Mutagenesisi283D → E: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
    Mutagenesisi285Y → A: Reduction of the catalytic efficiency with carob galactomannan and 2,4-DNPM. 1 Publication1
    Mutagenesisi320E → A: Does not alter the affinity against carob galactomannan, azo-carob galactomannan, mannotetraose and 2,4-DNPM. Lack of activity against all substrates; when associated with A-283. 2 Publications1
    Mutagenesisi320E → D: Causes a dramatic decrease in the catalytic efficiency against mannotetraose. 1 Publication1
    Mutagenesisi320E → G: Lack of activity against all substrates. 2 Publications1
    Mutagenesisi360W → A: Lack of activity against all substrates. 1 Publication1
    Mutagenesisi361R → A: Strong decrease of mannanase activity against oligosaccharides, while the reduction in the rate of polysaccharide hydrolysis is more modest. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units; when associated with A-377. 1 Publication1
    Mutagenesisi377H → A: 100-fold decrease in the activity of the mannanase against mannotetraose and 4-nitrophenyl-beta-D-Man2. It hydrolyzes polysaccharides only 10-20-fold less efficiently than the wild-type. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units; when associated with A-361. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03814 2-(N-Morpholino)-Ethanesulfonic Acid
    DB04084 2-deoxy-2-fluoro-Alpha-D-mannose
    DB04483 2-deoxy-2-fluoro-Beta-D-mannose
    DB02680 Dinitrophenylene

    <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 – 27PROSITE-ProRule annotation1 PublicationAdd BLAST27
    <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_000001217328 – 423Mannan endo-1,4-beta-mannosidaseAdd BLAST396

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P49424

    <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

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    498211.CJA_2770

    <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

    1423
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P49424

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

    More...
    SMRi
    P49424

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P49424

    <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_and_domains_section">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>Domaini56 – 409GH26PROSITE-ProRule annotationAdd BLAST354

    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>Regioni360 – 361Substrate binding3 Publications2

    <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 26 family.PROSITE-ProRule annotationCurated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105D3P Bacteria
    COG4124 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000274384

    KEGG Orthology (KO)

    More...
    KOi
    K01218

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CDYARGW

    Database of Orthologous Groups

    More...
    OrthoDBi
    POG091H0E82

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR022790 GH26_dom
    IPR000805 Glyco_hydro_26
    IPR017853 Glycoside_hydrolase_SF

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR40079 PTHR40079, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02156 Glyco_hydro_26, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00739 GLHYDRLASE26

    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
    PS51764 GH26, 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.

    P49424-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTITTARLP WAAQSFALGI CLIALLGCNH AANKSSASRA DVKPVTVKLV
    60 70 80 90 100
    DSQATMETRS LFAFMQEQRR HSIMFGHQHE TTQGLTITRT DGTQSDTFNA
    110 120 130 140 150
    VGDFAAVYGW DTLSIVAPKA EGDIVAQVKK AYARGGIITV SSHFDNPKTD
    160 170 180 190 200
    TQKGVWPVGT SWDQTPAVVD SLPGGAYNPV LNGYLDQVAE WANNLKDEQG
    210 220 230 240 250
    RLIPVIFRLY HENTGSWFWW GDKQSTPEQY KQLFRYSVEY LRDVKGVRNF
    260 270 280 290 300
    LYAYSPNNFW DVTEANYLER YPGDEWVDVL GFDTYGPVAD NADWFRNVVA
    310 320 330 340 350
    NAALVARMAE ARGKIPVISE IGIRAPDIEA GLYDNQWYRK LISGLKADPD
    360 370 380 390 400
    AREIAFLLVW RNAPQGVPGP NGTQVPHYWV PANRPENINN GTLEDFQAFY
    410 420
    ADEFTAFNRD IEQVYQRPTL IVK
    Length:423
    Mass (Da):47,487
    Last modified:July 5, 2005 - v2
    <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:iEFDAB597F10BA3DD
    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
    X82179 Genomic DNA Translation: CAA57670.2
    CP000934 Genomic DNA Translation: ACE82849.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S53374

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_012488364.1, NC_010995.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ACE82849; ACE82849; CJA_2770

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cja:CJA_2770

    <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
    X82179 Genomic DNA Translation: CAA57670.2
    CP000934 Genomic DNA Translation: ACE82849.1
    PIRiS53374
    RefSeqiWP_012488364.1, NC_010995.1

    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
    1GVYX-ray1.70A39-422[»]
    1GW1X-ray1.65A43-421[»]
    1J9YX-ray1.85A39-423[»]
    1ODZX-ray1.40A/B39-423[»]
    1R7OX-ray1.85A29-423[»]
    2WHMX-ray1.50A39-423[»]
    ProteinModelPortaliP49424
    SMRiP49424
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi498211.CJA_2770

    Chemistry databases

    DrugBankiDB03814 2-(N-Morpholino)-Ethanesulfonic Acid
    DB04084 2-deoxy-2-fluoro-Alpha-D-mannose
    DB04483 2-deoxy-2-fluoro-Beta-D-mannose
    DB02680 Dinitrophenylene

    Protein family/group databases

    CAZyiGH26 Glycoside Hydrolase Family 26

    Proteomic databases

    PRIDEiP49424

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACE82849; ACE82849; CJA_2770
    KEGGicja:CJA_2770

    Phylogenomic databases

    eggNOGiENOG4105D3P Bacteria
    COG4124 LUCA
    HOGENOMiHOG000274384
    KOiK01218
    OMAiCDYARGW
    OrthoDBiPOG091H0E82

    Enzyme and pathway databases

    BioCyciCJAP498211:G1GB3-2766-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP49424

    Family and domain databases

    InterProiView protein in InterPro
    IPR022790 GH26_dom
    IPR000805 Glyco_hydro_26
    IPR017853 Glycoside_hydrolase_SF
    PANTHERiPTHR40079 PTHR40079, 1 hit
    PfamiView protein in Pfam
    PF02156 Glyco_hydro_26, 1 hit
    PRINTSiPR00739 GLHYDRLASE26
    SUPFAMiSSF51445 SSF51445, 1 hit
    PROSITEiView protein in PROSITE
    PS51764 GH26, 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 nameiMANA_CELJU
    <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: P49424
    Secondary accession number(s): B3PBK3
    <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: February 1, 1996
    Last sequence update: July 5, 2005
    Last modified: December 5, 2018
    This is version 102 of the entry and version 2 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 programProkaryotic 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, Direct protein sequencing, Reference proteome

    Documents

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