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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei41 – 411NucleophilePROSITE-ProRule annotation
Binding sitei57 – 571Substrate
Binding sitei65 – 651Substrate
Binding sitei103 – 1031Substrate; via amide nitrogen
Active sitei241 – 2411Proton donor/acceptorPROSITE-ProRule annotation
Binding sitei241 – 2411Substrate
Binding sitei335 – 3351Substrate

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 537518Extracellular exo-inulinase inuEPRO_5000067603Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)Sequence analysis
Glycosylationi67 – 671N-linked (GlcNAc...)1 Publication
Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence analysis
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)1 Publication
Glycosylationi398 – 3981N-linked (GlcNAc...)1 Publication
Glycosylationi430 – 4301N-linked (GlcNAc...)1 Publication

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

1
537
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Beta strandi35 – 4814Combined sources
Beta strandi51 – 588Combined sources
Beta strandi63 – 653Combined sources
Beta strandi69 – 8012Combined sources
Beta strandi82 – 887Combined sources
Turni92 – 943Combined sources
Beta strandi99 – 10810Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi124 – 13411Combined sources
Beta strandi148 – 15811Combined sources
Turni167 – 1693Combined sources
Helixi181 – 1833Combined sources
Beta strandi186 – 19510Combined sources
Turni196 – 1994Combined sources
Beta strandi200 – 2078Combined sources
Helixi208 – 2103Combined sources
Beta strandi212 – 22312Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi237 – 25014Combined sources
Turni251 – 2544Combined sources
Beta strandi256 – 26611Combined sources
Beta strandi276 – 2849Combined sources
Beta strandi289 – 2913Combined sources
Turni293 – 2953Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi313 – 3175Combined sources
Helixi323 – 3253Combined sources
Beta strandi327 – 3315Combined sources
Turni335 – 3373Combined sources
Helixi338 – 3403Combined sources
Beta strandi344 – 3474Combined sources
Beta strandi354 – 3618Combined sources
Beta strandi364 – 3718Combined sources
Helixi375 – 3773Combined sources
Beta strandi384 – 3929Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi404 – 41310Combined sources
Beta strandi417 – 42711Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi435 – 4406Combined sources
Turni441 – 4444Combined sources
Beta strandi445 – 4495Combined sources
Turni460 – 4623Combined sources
Beta strandi465 – 4695Combined sources
Beta strandi476 – 48510Combined sources
Beta strandi488 – 4936Combined sources
Turni494 – 4974Combined sources
Beta strandi498 – 5036Combined sources
Beta strandi512 – 5209Combined sources
Beta strandi522 – 53211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4WX-ray1.55A20-537[»]
1Y9GX-ray1.87A20-537[»]
1Y9MX-ray1.89A20-537[»]
ProteinModelPortaliQ96TU3.
SMRiQ96TU3. Positions 20-536.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96TU3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 412Substrate binding
Regioni188 – 1892Substrate binding

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4WX-ray1.55A20-537[»]
1Y9GX-ray1.87A20-537[»]
1Y9MX-ray1.89A20-537[»]
ProteinModelPortaliQ96TU3.
SMRiQ96TU3. Positions 20-536.
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: October 14, 2015
This is version 66 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.