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Entry version 79 (11 Dec 2019)
Sequence version 1 (24 Jan 2006)
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Protein

Exo-1,4-beta-xylosidase xlnD

Gene

xlnD

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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.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-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>pH dependencei

Optimum pH is 4.0. Stable in the wide pH range of 3.0 to 7.0.1 Publication

Temperature dependencei

Stable at temperatures of up to 45 degrees Celsius and is inactivated gradually above 45 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei310By 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

  • ferric iron binding Source: InterPro
  • xylan 1,4-beta-xylosidase activity Source: AspGD

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

<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:
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:xyl-1, xylA
ORF Names:AO090005000986
<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 oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
<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 identifieri510516 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006564 <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 1

<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 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 – 20Sequence analysisAdd BLAST20
<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_000039329121 – 798Exo-1,4-beta-xylosidase xlnDAdd BLAST778

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>Glycosylationi23N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi87N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi142N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi237N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi326N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi391N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi404N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi443N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi480N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi522N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi618N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi645N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi658N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi685N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi707N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

<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

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

More...
SMRi
Q2UR38

Database of comparative protein structure models

More...
ModBasei
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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000031216

KEGG Orthology (KO)

More...
KOi
K15920

Identification of Orthologs from Complete Genome Data

More...
OMAi
YYTPQFL

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
IPR002024 Bacterioferritin
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
PF14310 Fn3-like, 1 hit
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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q2UR38-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPGAASIVAV LAALLPTALG QANQSYVDYN IEANPDLFSE CLETGGTSFP
60 70 80 90 100
DCESGPLSKT LVCDTSAKPH DRAAALVSLL TFEELVNNTA NTGHGAPRIG
110 120 130 140 150
LPAYQVWNEA LHGVAHADFS DAGGFSWSTS FPQPISTMAA LNRTLIHQIA
160 170 180 190 200
TIISTQGRAF MNAGRYGLDV YSPNINTFRH PVWGRGQETP GEDAYCLAST
210 220 230 240 250
YAYEYITGIQ GGVDANPLKL IATAKHYAGY DIENWDNHSR LGNDMQITQQ
260 270 280 290 300
DLAEYYTPQF LVASRDAKVH SVMCSYNAVN GVPSCSNSFF LQTLLRDTFD
310 320 330 340 350
FVEDGYVSGD CGAVYNVFNP HGYATNESSA AADSIRAGTD IDCGVSYPRH
360 370 380 390 400
FQESFHDQEV SRQDLERGVT RLYASLIRAG YFDGKTSPYR NITWSDVVST
410 420 430 440 450
NAQNLSYEAA AQSIVLLKND GILPLTSTSS STKTIALIGP WANATTQMLG
460 470 480 490 500
NYYGPAPYLI SPLQAFQDSE YKITYTIGTN TTTDPDSTSQ STALTTAKEA
510 520 530 540 550
DLIIFAGGID NTLETEAQDR SNITWPSNQL SLITKLADLG KPLIVLQMGG
560 570 580 590 600
GQVDSSALKN NKNVNALIWG GYPGQSGGQA LADIITGKRA PAARLVTTQY
610 620 630 640 650
PAEYAEVFPA IDMNLRPNGS NPGQTYMWYT GTPVYEFGHG LFYTNFTASA
660 670 680 690 700
SASSGTKNRT SFNIDEVLGR PHLGYKLVEQ MPLLNFTVDV KNTGDRVSDY
710 720 730 740 750
TAMAFVNTTA GPAPHPNKWL VGFDRLSAVE PGSAKTMVIP VTVDSLARTD
760 770 780 790
EEGNRVLYPG RYEVALNNER EVVLGFTLTG EKAVLFKWPK EEQLIAPQ
Length:798
Mass (Da):86,452
Last modified:January 24, 2006 - 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:iA8BE212A0A93C5E0
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 conflicti31I → S in BAA24107 (Ref. 1) Curated1
Sequence conflicti124G → D in BAA24107 (Ref. 1) Curated1
Sequence conflicti124G → D in BAA28267 (PubMed:9872754).Curated1
Sequence conflicti370T → I in BAA24107 (Ref. 1) Curated1
Sequence conflicti370T → I in BAA28267 (PubMed:9872754).Curated1
Sequence conflicti653S → G in BAA24107 (Ref. 1) Curated1
Sequence conflicti653S → G in BAA28267 (PubMed:9872754).Curated1
Sequence conflicti673L → P in BAA24107 (Ref. 1) Curated1
Sequence conflicti673L → P in BAA28267 (PubMed:9872754).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
AB009972 Genomic DNA Translation: BAA24107.1
AB013851 Genomic DNA Translation: BAA28267.1
AP007151 Genomic DNA Translation: BAE55977.1

NCBI Reference Sequences

More...
RefSeqi
XP_001817979.1, XM_001817927.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
BAE55977; BAE55977; AO090005000986

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5990515

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
aor:AO090005000986

<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
AB009972 Genomic DNA Translation: BAA24107.1
AB013851 Genomic DNA Translation: BAA28267.1
AP007151 Genomic DNA Translation: BAE55977.1
RefSeqiXP_001817979.1, XM_001817927.1

3D structure databases

SMRiQ2UR38
ModBaseiSearch...

Protein family/group databases

CAZyiGH3 Glycoside Hydrolase Family 3

Genome annotation databases

EnsemblFungiiBAE55977; BAE55977; AO090005000986
GeneIDi5990515
KEGGiaor:AO090005000986

Phylogenomic databases

HOGENOMiHOG000031216
KOiK15920
OMAiYYTPQFL

Enzyme and pathway databases

UniPathwayiUPA00114

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
IPR002024 Bacterioferritin
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
PF14310 Fn3-like, 1 hit
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...

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 nameiXYND_ASPOR
<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: Q2UR38
Secondary accession number(s): O42698, O59862
<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: January 24, 2006
Last modified: December 11, 2019
This is version 79 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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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