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O00105 (IPUA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isopullulanase

EC=3.2.1.57
Gene names
Name:ipuA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes pullulan, a linear polymer which is composed of maltotriose units with alpha-1,6 glucosidic linkages, to produce isopanose (Glca1-4Glca1-6Glc).

Catalytic activity

Hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose).

Subcellular location

Secreted.

Post-translational modification

N-glycosylated.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionisopullulanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 564545Isopullulanase
PRO_0000021520

Amino acid modifications

Glycosylation241N-linked (GlcNAc...)
Glycosylation941N-linked (GlcNAc...)
Glycosylation1151N-linked (GlcNAc...)
Glycosylation1381N-linked (GlcNAc...)
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...)
Glycosylation3051N-linked (GlcNAc...)
Glycosylation3811N-linked (GlcNAc...)
Glycosylation4481N-linked (GlcNAc...)
Glycosylation4551N-linked (GlcNAc...)
Glycosylation4601N-linked (GlcNAc...)
Glycosylation4861N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...)
Glycosylation5031N-linked (GlcNAc...)
Glycosylation5351N-linked (GlcNAc...)

Secondary structure

................................................................................................................... 564
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00105 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B6C0B70BF737CC40

FASTA56461,449
        10         20         30         40         50         60 
MRSTGYLLTL SAAFQVAQAA VTANNSQLLT WWHNTGEINT QTPVADGNVR QSGLYSVKVQ 

        70         80         90        100        110        120 
TTPASSSLYY DSFVYLAIPG NGMSDQLQYT QGYNQTQAWT SFLYSHDATV KISRNGSSAN 

       130        140        150        160        170        180 
SNVVIRPTSL NFPVRYDNQS VYITVPYSPT GYRFSVEFDD DLISLAPSGA RQPENALLIF 

       190        200        210        220        230        240 
ASPFENSSTK PQPGSPNSIA PAPGRVLGLN TTSASTVVFN PGVYYFTGHD HMVLSSSVTW 

       250        260        270        280        290        300 
VYFAPGAYVK GAVEFLSTAS EVKASGHGVL SGEQYVWYAD PDEGYQKASG ANNNGLRMWR 

       310        320        330        340        350        360 
GTLGNSSQTF VLNGVTVSAP PFNSMDWSGN SLDLITCRVD DYKQVGAFYG QTDGLEMYPG 

       370        380        390        400        410        420 
TILQDVFYHT DDDGLKMYYS NVTARNIVMW KESVAPVVEF GWTPRNTENV LFDNVDVIHQ 

       430        440        450        460        470        480 
AYANAGNNPG IFGAVNNYLY APDGLSSNHS TGNSNMTVRN ITWSNFRAEG SSSALFRINP 

       490        500        510        520        530        540 
IQNLDNISIK NVSIESFEPL SINTTESWMP VWYDLNNGKQ ITVTDFSIEG FTVGNTTITA 

       550        560 
SNAASVGRID GVDPAYAGSV HYID 

« Hide

References

[1]"Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger ATCC 9642."
Aoki H., Yopi X., Sakano Y.
Biochem. J. 323:757-764(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9642 / CBS 246.65 / DSM 63263 / IFO 6342 / NRRL 3536.
[2]"Two components of cell-bound isopullulanase from Aspergillus niger ATCC 9642 -- their purification and enzymatic properties."
Aoki H., Yopi X., Padmajanti A., Sakano Y.
Biosci. Biotechnol. Biochem. 60:1795-1798(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-29, CHARACTERIZATION.
Strain: ATCC 9642 / CBS 246.65 / DSM 63263 / IFO 6342 / NRRL 3536.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB001940 Genomic DNA. Translation: BAA19473.1.
D85240 Genomic DNA. Translation: BAA18971.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WMRX-ray2.40A/B20-564[»]
1X0CX-ray1.70A/B20-564[»]
2Z8GX-ray1.70A/B20-564[»]
ProteinModelPortalO00105.
SMRO00105. Positions 20-564.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH49. Glycoside Hydrolase Family 49.
mycoCLAPIPU49A_ASPNG.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.160.20.10. 1 hit.
2.60.350.10. 1 hit.
InterProIPR005192. Glyco_hydro_49.
IPR023226. Glyco_hydro_49_N_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamPF03718. Glyco_hydro_49. 1 hit.
[Graphical view]
SUPFAMSSF101596. SSF101596. 1 hit.
SSF51126. SSF51126. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO00105.

Entry information

Entry nameIPUA_ASPNG
AccessionPrimary (citable) accession number: O00105
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: July 1, 1997
Last modified: November 13, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries