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UniProtKB - Q96TU3 (INUE_ASPAW)
Protein
Extracellular exo-inulinase inuE
Gene
inuE
Organism
Aspergillus awamori (Black koji mold)
Status
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 PublicationCatalytic activityi
- Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.1 Publication EC:3.2.1.80
Kineticsi
- KM=0.003 mM for inulin1 Publication
- KM=10.1 mM for stachyose1 Publication
- KM=8 mM for raffinose1 Publication
- Vmax=175 µmol/min/mg enzyme toward inulin1 Publication
- Vmax=1.2 µmol/min/mg enzyme toward levan1 Publication
- Vmax=80 µmol/min/mg enzyme toward stachyose1 Publication
- Vmax=120 µmol/min/mg enzyme toward raffinose1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 41 | NucleophilePROSITE-ProRule annotation | 1 | |
Binding sitei | 57 | Substrate | 1 | |
Binding sitei | 65 | Substrate | 1 | |
Binding sitei | 103 | Substrate; via amide nitrogen | 1 | |
Active sitei | 241 | Proton donor/acceptorPROSITE-ProRule annotation | 1 | |
Binding sitei | 241 | Substrate | 1 | |
Binding sitei | 335 | Substrate | 1 |
GO - Molecular functioni
- fructan beta-fructosidase activity Source: UniProtKB-EC
GO - Biological processi
- polysaccharide catabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Biological process | Carbohydrate metabolism, Polysaccharide degradation |
Enzyme and pathway databases
BRENDAi | 3.2.1.80, 494 |
Protein family/group databases
CAZyi | GH32, Glycoside Hydrolase Family 32 |
CLAEi | INX32A_ASPAW |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:inuE Synonyms:inu1 |
Organismi | Aspergillus awamori (Black koji mold) |
Taxonomic identifieri | 105351 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus |
Subcellular locationi
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 19 | 1 PublicationAdd BLAST | 19 | |
ChainiPRO_5000067603 | 20 – 537 | Extracellular exo-inulinase inuEAdd BLAST | 518 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 49 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 67 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 111 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 112 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 254 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 300 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 398 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 430 | N-linked (GlcNAc...) asparagine1 Publication | 1 |
Keywords - PTMi
GlycoproteinPTM databases
iPTMneti | Q96TU3 |
Expressioni
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.
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q96TU3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q96TU3 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 40 – 41 | Substrate binding | 2 | |
Regioni | 188 – 189 | Substrate binding | 2 |
Sequence similaritiesi
Belongs to the glycosyl hydrolase 32 family.Curated
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 2.115.10.20, 1 hit |
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 |
Pfami | View protein in Pfam PF08244, Glyco_hydro_32C, 1 hit PF00251, Glyco_hydro_32N, 1 hit |
SMARTi | View protein in SMART SM00640, Glyco_32, 1 hit |
SUPFAMi | SSF49899, SSF49899, 1 hit SSF75005, SSF75005, 1 hit |
PROSITEi | View protein in PROSITE PS00609, GLYCOSYL_HYDROL_F32, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q96TU3-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ315793 Genomic DNA Translation: CAC44220.1 |
Similar proteinsi
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: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1Y4W | X-ray | 1.55 | A | 20-537 | [»] | |
1Y9G | X-ray | 1.87 | A | 20-537 | [»] | |
1Y9M | X-ray | 1.89 | A | 20-537 | [»] | |
SMRi | Q96TU3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
CAZyi | GH32, Glycoside Hydrolase Family 32 |
CLAEi | INX32A_ASPAW |
PTM databases
iPTMneti | Q96TU3 |
Enzyme and pathway databases
BRENDAi | 3.2.1.80, 494 |
Miscellaneous databases
EvolutionaryTracei | Q96TU3 |
Family and domain databases
Gene3Di | 2.115.10.20, 1 hit |
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 |
Pfami | View protein in Pfam PF08244, Glyco_hydro_32C, 1 hit PF00251, Glyco_hydro_32N, 1 hit |
SMARTi | View protein in SMART SM00640, Glyco_32, 1 hit |
SUPFAMi | SSF49899, SSF49899, 1 hit SSF75005, SSF75005, 1 hit |
PROSITEi | View protein in PROSITE PS00609, GLYCOSYL_HYDROL_F32, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | INUE_ASPAW | |
Accessioni | Q96TU3Primary (citable) accession number: Q96TU3 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families