Exo-inulinase precursor - Aspergillus awamori

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Unreviewed, UniProtKB/TrEMBL Q96TU3 (Q96TU3_ASPAW)

Last modified April 14, 2009. Version 31. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Submitted name:
Exo-inulinase EMBL CAC44220.1
EC=3.2.1.80

Gene names

Name:

inu1 EMBL CAC44220.1

Organism

Aspergillus awamori EMBL CAC44220.1

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 32 family. RuleBase RU000449V1

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase RuleBase RU000449V1 Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	fructan beta-fructosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

19

EMBL CAC44220.1

Chain

518

Potential EMBL CAC44220.1

PRO_5000067603

Chain

499

inulinase EMBL CAC44220.1

PRO_5000067604

Sequences

Sequence

Length

Mass (Da)

Tools

Q96TU3-1 [UniParc].

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

537

59,171

        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

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

AJ315793 Genomic DNA. Translation: CAC44220.1.

3D structure databases

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	[»]

ModBase

Protein family/group databases

CAZy

GH32. Glycoside Hydrolase Family 32.

Enzyme and pathway databases

BRENDA

3.2.1.80. 15245.

Family and domain databases

InterPro

IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
[Graphical view]

Pfam

PF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]

SMART

SM00640. Glyco_32. 1 hit.
[Graphical view]

PROSITE

PS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

Q96TU3_ASPAW

Accession

Primary (citable) accession number: Q96TU3

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	April 14, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information