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UniProtKB - Q96TU3 (INUE_ASPAW)

Entry version 79 (02 Jun 2021)
Sequence version 1 (01 Dec 2001)
Previous versions | rss
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Protein

Extracellular exo-inulinase inuE

Gene

inuE

Organism
Aspergillus awamori (Black koji mold)
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

Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyzes levan, stachyose and raffinose.

1 Publication

<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=0.003 mM for inulin1 Publication
  2. KM=10.1 mM for stachyose1 Publication
  3. KM=8 mM for raffinose1 Publication
  1. Vmax=175 µmol/min/mg enzyme toward inulin1 Publication
  2. Vmax=1.2 µmol/min/mg enzyme toward levan1 Publication
  3. Vmax=80 µmol/min/mg enzyme toward stachyose1 Publication
  4. Vmax=120 µmol/min/mg enzyme toward raffinose1 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 sitei41NucleophilePROSITE-ProRule annotation1
<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 sitei57Substrate1
Binding sitei65Substrate1
Binding sitei103Substrate; via amide nitrogen1
Active sitei241Proton donor/acceptorPROSITE-ProRule annotation1
Binding sitei241Substrate1
Binding sitei335Substrate1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.2.1.80, 494

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GH32, Glycoside Hydrolase Family 32

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

More...CLAEi		INX32A_ASPAW

<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:
Extracellular exo-inulinase inuE (EC:3.2.1.80)
<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:inuE
Synonyms:inu1
<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>OrganismiAspergillus awamori (Black koji mold)
<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 identifieri105351 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus

<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

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 – 191 PublicationAdd BLAST19
<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_500006760320 – 537Extracellular exo-inulinase inuEAdd BLAST518

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi49N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi67N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi111N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi112N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi254N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi300N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi398N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi430N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Glycoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q96TU3

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is induced in presence of maltose, sucrose or inulin and controlled by the catabolite repressor creA and by the inulinolytic genes regulator inuR.

<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

1537
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		Q96TU3

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		Q96TU3

<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

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>Regioni40 – 41Substrate binding2
Regioni188 – 189Substrate binding2

<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 32 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.115.10.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013320, ConA-like_dom_sf
IPR001362, Glyco_hydro_32
IPR018053, Glyco_hydro_32_AS
IPR013189, Glyco_hydro_32_C
IPR013148, Glyco_hydro_32_N
IPR023296, Glyco_hydro_beta-prop_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08244, Glyco_hydro_32C, 1 hit
PF00251, Glyco_hydro_32N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00640, Glyco_32, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49899, SSF49899, 1 hit
SSF75005, SSF75005, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00609, GLYCOSYL_HYDROL_F32, 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.

Q96TU3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPLSKALSV FMLMGITYAF NYDQPYRGQY HFSPQKNWMN DPNGLLYHNG 
        60         70         80         90        100
TYHLFFQYNP GGIEWGNISW GHAISEDLTH WEEKPVALLA RGFGSDVTEM 
       110        120        130        140        150
YFSGSAVADV NNTSGFGKDG KTPLVAMYTS YYPVAQTLPS GQTVQEDQQS 
       160        170        180        190        200
QSIAYSLDDG LTWTTYDAAN PVIPNPPSPY EAEYQNFRDP FVFWHDESQK 
       210        220        230        240        250
WVVVTSIAEL HKLAIYTSDN LKDWKLVSEF GPYNAQGGVW ECPGLVKLPL 
       260        270        280        290        300
DSGNSTKWVI TSGLNPGGPP GTVGSGTQYF VGEFDGTTFT PDADTVYPGN 
       310        320        330        340        350
STANWMDWGP DFYAAAGYNG LSLNDHVHIG WMNNWQYGAN IPTYPWRSAM 
       360        370        380        390        400
AIPRHMALKT IGSKATLVQQ PQEAWSSISN KRPIYSRTFK TLSEGSTNTT 
       410        420        430        440        450
TTGETFKVDL SFSAKSKAST FAIALRASAN FTEQTLVGYD FAKQQIFLDR 
       460        470        480        490        500
THSGDVSFDE TFASVYHGPL TPDSTGVVKL SIFVDRSSVE VFGGQGETTL 
       510        520        530 
TAQIFPSSDA VHARLASTGG TTEDVRADIY KIASTWN
Length:537
Mass (Da):59,171
Last modified:December 1, 2001 - 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:i1575700AF21D070B
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
AJ315793 Genomic DNA Translation: CAC44220.1

<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
AJ315793 Genomic DNA Translation: CAC44220.1

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
1Y4WX-ray1.55A20-537[»]
1Y9GX-ray1.87A20-537[»]
1Y9MX-ray1.89A20-537[»]
SMRiQ96TU3
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiGH32, Glycoside Hydrolase Family 32
CLAEiINX32A_ASPAW

PTM databases

iPTMnetiQ96TU3

Enzyme and pathway databases

BRENDAi3.2.1.80, 494

Miscellaneous databases

EvolutionaryTraceiQ96TU3

Family and domain databases

Gene3Di2.115.10.20, 1 hit
InterProiView protein in InterPro
IPR013320, ConA-like_dom_sf
IPR001362, Glyco_hydro_32
IPR018053, Glyco_hydro_32_AS
IPR013189, Glyco_hydro_32_C
IPR013148, Glyco_hydro_32_N
IPR023296, Glyco_hydro_beta-prop_sf
PfamiView protein in Pfam
PF08244, Glyco_hydro_32C, 1 hit
PF00251, Glyco_hydro_32N, 1 hit
SMARTiView protein in SMART
SM00640, Glyco_32, 1 hit
SUPFAMiSSF49899, SSF49899, 1 hit
SSF75005, SSF75005, 1 hit
PROSITEiView protein in PROSITE
PS00609, GLYCOSYL_HYDROL_F32, 1 hit

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 nameiINUE_ASPAW
<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: Q96TU3
<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: July 9, 2014
Last sequence update: December 1, 2001
Last modified: June 2, 2021
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

3D-structure, Direct protein sequencing

Documents

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