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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-Experimental evidence at protein leveli

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

Catalytic activityi

Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.1 Publication

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
Active sitei41NucleophilePROSITE-ProRule annotation1
Binding sitei57Substrate1
Binding sitei65Substrate1
Binding sitei103Substrate; via amide nitrogen1
Active sitei241Proton donor/acceptorPROSITE-ProRule annotation1
Binding sitei241Substrate1
Binding sitei335Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.80. 494.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.
mycoCLAPiINX32A_ASPAW.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular exo-inulinase inuE (EC:3.2.1.80)
Gene namesi
Name:inuE
Synonyms:inu1
OrganismiAspergillus awamori (Black koji mold)
Taxonomic identifieri105351 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_500006760320 – 537Extracellular exo-inulinase inuEAdd BLAST518

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi49N-linked (GlcNAc...)Sequence analysis1
Glycosylationi67N-linked (GlcNAc...)1 Publication1
Glycosylationi111N-linked (GlcNAc...)1 Publication1
Glycosylationi112N-linked (GlcNAc...)Sequence analysis1
Glycosylationi254N-linked (GlcNAc...)Sequence analysis1
Glycosylationi300N-linked (GlcNAc...)1 Publication1
Glycosylationi398N-linked (GlcNAc...)1 Publication1
Glycosylationi430N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Glycoprotein

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

1537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 31Combined sources3
Beta strandi35 – 48Combined sources14
Beta strandi51 – 58Combined sources8
Beta strandi63 – 65Combined sources3
Beta strandi69 – 80Combined sources12
Beta strandi82 – 88Combined sources7
Turni92 – 94Combined sources3
Beta strandi99 – 108Combined sources10
Beta strandi113 – 115Combined sources3
Beta strandi119 – 121Combined sources3
Beta strandi124 – 134Combined sources11
Beta strandi148 – 158Combined sources11
Turni167 – 169Combined sources3
Helixi181 – 183Combined sources3
Beta strandi186 – 195Combined sources10
Turni196 – 199Combined sources4
Beta strandi200 – 207Combined sources8
Helixi208 – 210Combined sources3
Beta strandi212 – 223Combined sources12
Beta strandi225 – 230Combined sources6
Beta strandi237 – 250Combined sources14
Turni251 – 254Combined sources4
Beta strandi256 – 266Combined sources11
Beta strandi276 – 284Combined sources9
Beta strandi289 – 291Combined sources3
Turni293 – 295Combined sources3
Beta strandi298 – 301Combined sources4
Beta strandi304 – 306Combined sources3
Beta strandi308 – 311Combined sources4
Beta strandi313 – 317Combined sources5
Helixi323 – 325Combined sources3
Beta strandi327 – 331Combined sources5
Turni335 – 337Combined sources3
Helixi338 – 340Combined sources3
Beta strandi344 – 347Combined sources4
Beta strandi354 – 361Combined sources8
Beta strandi364 – 371Combined sources8
Helixi375 – 377Combined sources3
Beta strandi384 – 392Combined sources9
Beta strandi394 – 396Combined sources3
Beta strandi404 – 413Combined sources10
Beta strandi417 – 427Combined sources11
Beta strandi431 – 433Combined sources3
Beta strandi435 – 440Combined sources6
Turni441 – 444Combined sources4
Beta strandi445 – 449Combined sources5
Turni460 – 462Combined sources3
Beta strandi465 – 469Combined sources5
Beta strandi476 – 485Combined sources10
Beta strandi488 – 493Combined sources6
Turni494 – 497Combined sources4
Beta strandi498 – 503Combined sources6
Beta strandi512 – 520Combined sources9
Beta strandi522 – 532Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y4WX-ray1.55A20-537[»]
1Y9GX-ray1.87A20-537[»]
1Y9MX-ray1.89A20-537[»]
ProteinModelPortaliQ96TU3.
SMRiQ96TU3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96TU3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 41Substrate binding2
Regioni188 – 189Substrate binding2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i1575700AF21D070B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ315793 Genomic DNA. Translation: CAC44220.1.

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 entryMethodResolution (Å)ChainPositionsPDBsum
1Y4WX-ray1.55A20-537[»]
1Y9GX-ray1.87A20-537[»]
1Y9MX-ray1.89A20-537[»]
ProteinModelPortaliQ96TU3.
SMRiQ96TU3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.
mycoCLAPiINX32A_ASPAW.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.80. 494.

Miscellaneous databases

EvolutionaryTraceiQ96TU3.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiINUE_ASPAW
AccessioniPrimary (citable) accession number: Q96TU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.