Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q96TU3 (Q96TU3_ASPAW) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesSubmitted name:
Exo-inulinase EMBL CAC44220.1
EC=3.2.1.80 EMBL CAC44220.1
Gene names
Name:inu1 EMBL CAC44220.1
OrganismAspergillus awamori (Black koji mold) EMBL CAC44220.1
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 32 family. RuleBase RU000449

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 EMBL CAC44220.1
Chain20 – 537518 Potential EMBL CAC44220.1
PRO_5000067603
Chain20 – 518499inulinase EMBL CAC44220.1
PRO_5000067604

Regions

Region40 – 412Fructose binding PDB 1Y9G
Region188 – 1892Fructose binding PDB 1Y9G

Sites

Binding site571Fructose PDB 1Y9G
Binding site651Fructose PDB 1Y9G
Binding site1031Fructose; via amide nitrogen PDB 1Y9G
Binding site2411Fructose PDB 1Y9G
Binding site3351Fructose PDB 1Y9G

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) PDB 1Y9G PDB 1Y9M PDB 1Y4W
Glycosylation1111N-linked (GlcNAc...) PDB 1Y9G PDB 1Y9M PDB 1Y4W
Glycosylation3001N-linked (GlcNAc...) PDB 1Y9M
Glycosylation3981N-linked (GlcNAc...) PDB 1Y9G PDB 1Y9M PDB 1Y4W
Glycosylation4301N-linked (GlcNAc...) PDB 1Y9G PDB 1Y9M PDB 1Y4W

Sequences

Sequence LengthMass (Da)Tools
Q96TU3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1575700AF21D070B

FASTA53759,171
        10         20         30         40         50         60 
MAPLSKALSV FMLMGITYAF NYDQPYRGQY HFSPQKNWMN DPNGLLYHNG TYHLFFQYNP 

        70         80         90        100        110        120 
GGIEWGNISW GHAISEDLTH WEEKPVALLA RGFGSDVTEM YFSGSAVADV NNTSGFGKDG 

       130        140        150        160        170        180 
KTPLVAMYTS YYPVAQTLPS GQTVQEDQQS QSIAYSLDDG LTWTTYDAAN PVIPNPPSPY 

       190        200        210        220        230        240 
EAEYQNFRDP FVFWHDESQK WVVVTSIAEL HKLAIYTSDN LKDWKLVSEF GPYNAQGGVW 

       250        260        270        280        290        300 
ECPGLVKLPL DSGNSTKWVI TSGLNPGGPP GTVGSGTQYF VGEFDGTTFT PDADTVYPGN 

       310        320        330        340        350        360 
STANWMDWGP DFYAAAGYNG LSLNDHVHIG WMNNWQYGAN IPTYPWRSAM AIPRHMALKT 

       370        380        390        400        410        420 
IGSKATLVQQ PQEAWSSISN KRPIYSRTFK TLSEGSTNTT TTGETFKVDL SFSAKSKAST 

       430        440        450        460        470        480 
FAIALRASAN FTEQTLVGYD FAKQQIFLDR THSGDVSFDE TFASVYHGPL TPDSTGVVKL 

       490        500        510        520        530 
SIFVDRSSVE VFGGQGETTL TAQIFPSSDA VHARLASTGG TTEDVRADIY KIASTWN

« Hide

References

[1]"Exo-inulinase from Aspergillus awamori var. 2250: enzymatic properties, sequence analysis and preliminary X-ray data."
Arand M., Golubev A.M., Neto B.J.R., Polikarpov I., Wattiez R., Korneeva O.S., Eneyskaya E.V., Kulminskaya A.A., Shabalin K.A., Shishliannikov S.M., Chepurnaya O.V., Neustroev K.N.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Var. 2250 EMBL CAC44220.1.
Tissue: Mycelium EMBL CAC44220.1.
[2]"Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition."
Nagem R.A., Rojas A.L., Golubev A.M., Korneeva O.S., Eneyskaya E.V., Kulminskaya A.A., Neustroev K.N., Polikarpov I.
J. Mol. Biol. 344:471-480(2004) [PubMed: 15522299] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 20-537 IN COMPLEX WITH FRUCTOSE, GLYCOSYLATION AT ASN-67; ASN-111; ASN-300; ASN-398 AND ASN-430.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ315793 Genomic DNA. Translation: CAC44220.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4WX-ray1.55A20-537[»]
1Y9GX-ray1.87A20-537[»]
1Y9MX-ray1.89A20-537[»]
ProteinModelPortalQ96TU3.
SMRQ96TU3. Positions 20-536.
ModBaseSearch...

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.80. 15245.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_43_beta-prop.
[Graphical view]
Gene3DG3DSA:2.115.10.20. Glyco_hydro_43_beta-prop. 1 hit.
PfamPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
SSF75005. Glyco_hydro_43_beta-prop. 1 hit.
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ96TU3_ASPAW
AccessionPrimary (citable) accession number: Q96TU3
Entry history
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info