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Entry version 111 (08 May 2019)
Sequence version 1 (01 Oct 2000)
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Protein

Reducing end xylose-releasing exo-oligoxylanase

Gene

BH2105

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Hydrolyzes xylooligosaccharides with a degree of polymerization of greater than or equal to 3, releasing xylose from the reducing end. Only hydrolyzes the beta anomers of xylooligosaccharides, with inversion of anomeric configuration. Hydrolyzes the glucose and xylose-based trisaccharides where xylose is located at the -1 subsite, GXX, XXG and GXG. Does not hydrolyze xylan, chitosan, lichenan, curdlan or carboxymethylcellulose.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 (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides.1 Publication EC:3.2.1.156

<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=2.4 mM for X3 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  2. KM=5.0 mM for X4 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  3. KM=4.4 mM for X5 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  4. KM=18.5 mM for X6 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  5. KM=4.3 mM for X3 (in 0.1 M MOPS, pH 7.0, 30 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 6.2-7.3. Stable between pH 5.0 and 9.8 for 30 min at 30 degrees Celsius.2 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Stable up to 40 degrees Celsius.2 Publications

    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 sitei70Proton donorBy similarity1
    Active sitei263Proton acceptorBy 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, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-17885

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.2.1.156 661

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH8 Glycoside Hydrolase Family 8

    <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:
    Reducing end xylose-releasing exo-oligoxylanase1 Publication (EC:3.2.1.156)
    Short name:
    Rex1 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
    Ordered Locus Names:BH2105
    <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>OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    <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 identifieri272558 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    <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
    • UP000001258 <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>Mutagenesisi70E → A: Activity is 0.01% of wild type. 1 Publication1
    Mutagenesisi128D → A: Activity is 0.4% of wild type. 1 Publication1
    Mutagenesisi198Y → F: Has high levels of glycosynthase activity. Reduced hydrolase activity. 1 Publication1
    Mutagenesisi263D → A: Activity is 0.02% of wild type. Has glycosynthase activity. 3 Publications1
    Mutagenesisi263D → C or N: Has high levels of glycosynthase activity. Reduced hydrolase activity. 3 Publications1
    Mutagenesisi263D → G, L, P, S, T or V: Has glycosynthase activity. 3 Publications1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03389 alpha-D-Xylopyranose

    <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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003972351 – 388Reducing end xylose-releasing exo-oligoxylanaseAdd BLAST388

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9KB30

    <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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    272558.10174724

    <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

    1388
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1WU4X-ray1.35A1-388[»]
    1WU5X-ray2.20A1-388[»]
    1WU6X-ray1.45A1-388[»]
    2DROX-ray1.70A1-388[»]
    2DRQX-ray2.10A1-388[»]
    2DRRX-ray1.60A1-388[»]
    2DRSX-ray2.10A1-388[»]
    3A3VX-ray1.39A1-388[»]

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

    More...
    SMRi
    Q9KB30

    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
    Q9KB30

    <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 8 (cellulase D) family.Sequence analysis

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105EK5 Bacteria
    COG3405 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000112672

    KEGG Orthology (KO)

    More...
    KOi
    K15531

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    FDRLWKW

    Database of Orthologous Groups

    More...
    OrthoDBi
    636673at2

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.50.10.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008928 6-hairpin_glycosidase_sf
    IPR012341 6hp_glycosidase-like_sf
    IPR002037 Glyco_hydro_8

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01270 Glyco_hydro_8, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00735 GLHYDRLASE8

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48208 SSF48208, 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.

    Q9KB30-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKKTTEGAFY TREYRNLFKE FGYSEAEIQE RVKDTWEQLF GDNPETKIYY
    60 70 80 90 100
    EVGDDLGYLL DTGNLDVRTE GMSYGMMMAV QMDRKDIFDR IWNWTMKNMY
    110 120 130 140 150
    MTEGVHAGYF AWSCQPDGTK NSWGPAPDGE EYFALALFFA SHRWGDGDEQ
    160 170 180 190 200
    PFNYSEQARK LLHTCVHNGE GGPGHPMWNR DNKLIKFIPE VEFSDPSYHL
    210 220 230 240 250
    PHFYELFSLW ANEEDRVFWK EAAEASREYL KIACHPETGL APEYAYYDGT
    260 270 280 290 300
    PNDEKGYGHF FSDSYRVAAN IGLDAEWFGG SEWSAEEINK IQAFFADKEP
    310 320 330 340 350
    EDYRRYKIDG EPFEEKSLHP VGLIATNAMG SLASVDGPYA KANVDLFWNT
    360 370 380
    PVRTGNRRYY DNCLYLFAML ALSGNFKIWF PEGQEEEH
    Length:388
    Mass (Da):45,010
    Last modified:October 1, 2000 - 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:iC1EBA5B4A98C0E28
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2K → E AA sequence (PubMed:15491996).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    BA000004 Genomic DNA Translation: BAB05824.1
    AY137373 Genomic DNA Translation: AAN16076.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A83913

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_010898262.1, NC_002570.2

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAB05824; BAB05824; BAB05824

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bha:BH2105

    <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
    BA000004 Genomic DNA Translation: BAB05824.1
    AY137373 Genomic DNA Translation: AAN16076.1
    PIRiA83913
    RefSeqiWP_010898262.1, NC_002570.2

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WU4X-ray1.35A1-388[»]
    1WU5X-ray2.20A1-388[»]
    1WU6X-ray1.45A1-388[»]
    2DROX-ray1.70A1-388[»]
    2DRQX-ray2.10A1-388[»]
    2DRRX-ray1.60A1-388[»]
    2DRSX-ray2.10A1-388[»]
    3A3VX-ray1.39A1-388[»]
    SMRiQ9KB30
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272558.10174724

    Chemistry databases

    DrugBankiDB03389 alpha-D-Xylopyranose

    Protein family/group databases

    CAZyiGH8 Glycoside Hydrolase Family 8

    Proteomic databases

    PRIDEiQ9KB30

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB05824; BAB05824; BAB05824
    KEGGibha:BH2105

    Phylogenomic databases

    eggNOGiENOG4105EK5 Bacteria
    COG3405 LUCA
    HOGENOMiHOG000112672
    KOiK15531
    OMAiFDRLWKW
    OrthoDBi636673at2

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17885
    BRENDAi3.2.1.156 661

    Miscellaneous databases

    EvolutionaryTraceiQ9KB30

    Family and domain databases

    Gene3Di1.50.10.10, 1 hit
    InterProiView protein in InterPro
    IPR008928 6-hairpin_glycosidase_sf
    IPR012341 6hp_glycosidase-like_sf
    IPR002037 Glyco_hydro_8
    PfamiView protein in Pfam
    PF01270 Glyco_hydro_8, 1 hit
    PRINTSiPR00735 GLHYDRLASE8
    SUPFAMiSSF48208 SSF48208, 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 nameiREOX_BACHD
    <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: Q9KB30
    Secondary accession number(s): Q8GLI2
    <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: August 10, 2010
    Last sequence update: October 1, 2000
    Last modified: May 8, 2019
    This is version 111 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 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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