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Protein

Probable exo-1,4-beta-xylosidase xlnD

Gene

xlnD

Organism
Aspergillus japonicus
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

Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.By similarity1 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-xylans, to remove successive D-xylose residues from the non-reducing termini. EC:3.2.1.37

<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=314 µM for p-nitrophenyl (pNP)-beta-D-xylopyranoside1 Publication
  1. Vmax=114 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 4.0. Retains greater than 90 percent of its original activity between pH 2.0 and 7.0 at room temperature for 3 h.1 Publication

Temperature dependencei

Optimum temperature 70 degrees Celsius. Remains stable up to 60 degrees Celsius for 30 min, but loses activity at 80 degrees Celsius.1 Publication

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

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

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 sitei307By 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

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

More...
UniPathwayi
UPA00114

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH3 Glycoside Hydrolase Family 3

mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

More...
mycoCLAPi
XYL3A_ASPJA

<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:
Probable exo-1,4-beta-xylosidase xlnD (EC:3.2.1.37)
Alternative name(s):
1,4-beta-D-xylan xylohydrolase xlnD
Beta-xylosidase A
Beta-xylosidase xlnD
Xylobiase xlnD
<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:xlnD
Synonyms:xylA
<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 japonicus
<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 identifieri34381 [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 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; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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 – 17Sequence analysisAdd BLAST17
<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_000039328918 – 804Probable exo-1,4-beta-xylosidase xlnDAdd BLAST787

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>Glycosylationi20N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi115N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi139N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi234N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi243N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi349N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi382N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi404N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi433N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi485N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi489N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi621N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi652N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi666N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi688N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi710N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
B6EY09

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
B6EY09

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

More...
SMRi
B6EY09

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
3.20.20.300, 1 hit
3.40.50.1700, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026891 Fn3-like
IPR002772 Glyco_hydro_3_C
IPR036881 Glyco_hydro_3_C_sf
IPR001764 Glyco_hydro_3_N
IPR036962 Glyco_hydro_3_N_sf
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01217 Fn3_like, 1 hit

Superfamily database of structural and functional annotation

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

B6EY09-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVAALALLA LLPQALGQHN SSYVDYNVEA NPDLFPQCLD TISLSFPDCQ
60 70 80 90 100
SGPLSKNLVC DSTASPYDRA AALVSLFTLE ELIANTGNTS PGVPRLGLPP
110 120 130 140 150
YQVWSEALHG LARANFTDNG AYSWATSFPS PILSAAAFNR TLINQIASII
160 170 180 190 200
STQGRAFNNA GRFGLDVYSP NINTFRHPVW GRGQETPGED AYTLTAAYAY
210 220 230 240 250
EYITGIQGGV NPEHLKLAAT AKHFAGYDIE NWDNHSRLGN DVNITQQDLA
260 270 280 290 300
EYYTPQFLVA ARDAHVHSFM CSYNAVNGVP SCSNTFFLQT LLRDTFSFVD
310 320 330 340 350
HGYVSGDCGA VYGVFNPHGY AANEPSAAAD AILAGTDIDC GTSYQYHFNE
360 370 380 390 400
SITTGAVARD DIERGFIRLY ANLVELGYFD GNSSSSNPYR SLGWPDVQKT
410 420 430 440 450
DAWNISYEAA VEGIVLLKND GTLPLASPSE GKNKSIALIG PWANATTQLQ
460 470 480 490 500
GNYYGDAPYL ISPVDAFTAA GYTVHYAPGT EISTNSTANF SAALSAARAA
510 520 530 540 550
DTIVFLGGID NTIEAEAQDR SSIAWPGNQL ELISQLAAQK SDDQPLVVYQ
560 570 580 590 600
MGGGQVDSSA LKSNAKVNAL LWGGYPGQSG GLALRDILTG ARAPAGRLTT
610 620 630 640 650
TQYPAAYAES FSALDMNLRP NETTQNPGQT YMWYTGEPVY AFGHGLFYTT
660 670 680 690 700
FNASSAQAAK TKYTFNITDL TSAAHPDTTT VGQRTLFNFT ASITNSGQRD
710 720 730 740 750
SDYTALVYAN TSTAGPSPYP NKWLVGFDRL AAVAKEGGTA ELNVPVAVDR
760 770 780 790 800
LARVDEAGNT VLFPGRYEVA LNNEREVVVE VELVGEQVVL LKWPEEVQGV

AGDE
Length:804
Mass (Da):86,258
Last modified:December 16, 2008 - 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:iD12E982EF2227943
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
AB379633 Genomic DNA Translation: BAG82824.1

<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
AB379633 Genomic DNA Translation: BAG82824.1

3D structure databases

ProteinModelPortaliB6EY09
SMRiB6EY09
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH3 Glycoside Hydrolase Family 3
mycoCLAPiXYL3A_ASPJA

Proteomic databases

PRIDEiB6EY09

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00114

Family and domain databases

Gene3Di2.60.40.10, 1 hit
3.20.20.300, 1 hit
3.40.50.1700, 1 hit
InterProiView protein in InterPro
IPR026891 Fn3-like
IPR002772 Glyco_hydro_3_C
IPR036881 Glyco_hydro_3_C_sf
IPR001764 Glyco_hydro_3_N
IPR036962 Glyco_hydro_3_N_sf
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
PfamiView protein in Pfam
PF00933 Glyco_hydro_3, 1 hit
PF01915 Glyco_hydro_3_C, 1 hit
SMARTiView protein in SMART
SM01217 Fn3_like, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
SSF52279 SSF52279, 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 nameiXYND_ASPJA
<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: B6EY09
<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: March 23, 2010
Last sequence update: December 16, 2008
Last modified: December 5, 2018
This is version 35 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

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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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