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P56526 (AGLU_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 65. 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:
Alpha-glucosidase

EC=3.2.1.20
Alternative name(s):
Maltase
Gene names
Name:aglA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length985 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch.

Catalytic activity

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Post-translational modification

The O-linked saccharide is not identified, but is probably mannose.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

maltose alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.2
Chain26 – 985960Alpha-glucosidase
PRO_0000018576

Sites

Active site4901Nucleophile
Active site4931 By similarity
Active site6601Proton donor By similarity

Amino acid modifications

Glycosylation361O-linked (Man) Probable
Glycosylation1241N-linked (GlcNAc...) Ref.2
Glycosylation1431N-linked (GlcNAc...) Ref.2
Glycosylation2181N-linked (GlcNAc...) Ref.2
Glycosylation3471N-linked (GlcNAc...) Ref.2
Glycosylation4221N-linked (GlcNAc...) Ref.2
Glycosylation5061N-linked (GlcNAc...) Ref.2
Glycosylation5341N-linked (GlcNAc...) Ref.2
Glycosylation5371N-linked (GlcNAc...)
Glycosylation5451O-linked (Man) Probable
Glycosylation5501O-linked (Man) Probable
Glycosylation5591O-linked (Man) Probable
Glycosylation5601O-linked (Man) Probable
Glycosylation5611O-linked (Man) Probable
Glycosylation5621O-linked (Man) Probable
Glycosylation5711O-linked (Man) Probable
Glycosylation6011N-linked (GlcNAc...) Ref.2
Glycosylation6231N-linked (GlcNAc...) Ref.2
Glycosylation8351N-linked (GlcNAc...) Ref.2
Glycosylation8811N-linked (GlcNAc...) Ref.2
Glycosylation8951O-linked (Man) Probable
Glycosylation8991N-linked (GlcNAc...) Ref.2
Glycosylation9571N-linked (GlcNAc...) Ref.2
Glycosylation9701N-linked (GlcNAc...) Ref.2

Natural variations

Natural variant27 – 282TT → LL in strain: GN-8.
Natural variant421D → A in strain: GN-8.
Natural variant9291N → M in strain: GN-8.

Sequences

Sequence LengthMass (Da)Tools
P56526 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 9A18772AEB2E0927

FASTA985108,913
        10         20         30         40         50         60 
MVKLTHLLAR AWLVPLAYGA SQSLLSTTAP SQPQFTIPAS ADVGAQLIAN IDDPQAADAQ 

        70         80         90        100        110        120 
SVCPGYKASK VQHNSRGFTA SLQLAGRPCN VYGTDVESLT LSVEYQDSDR LNIQILPTHV 

       130        140        150        160        170        180 
DSTNASWYFL SENLVPRPKA SLNASVSQSD LFVSWSNEPS FNFKVIRKAT GDALFSTEGT 

       190        200        210        220        230        240 
VLVYENQFIE FVTALPEEYN LYGLGEHITQ FRLQRNANLT IYPSDDGTPI DQNLYGQHPF 

       250        260        270        280        290        300 
YLDTRYYKGD RQNGSYIPVK SSEADASQDY ISLSHGVFLR NSHGLEILLR SQKLIWRTLG 

       310        320        330        340        350        360 
GGIDLTFYSG PAPADVTRQY LTSTVGLPAM QQYNTLGFHQ CRWGYNNWSD LADVVANFEK 

       370        380        390        400        410        420 
FEIPLEYIWT DIDYMHGYRN FDNDQHRFSY SEGDEFLSKL HESGRYYVPI VDAALYIPNP 

       430        440        450        460        470        480 
ENASDAYATY DRGAADDVFL KNPDGSLYIG AVWPGYTVFP DWHHPKAVDF WANELVIWSK 

       490        500        510        520        530        540 
KVAFDGVWYD MSEVSSFCVG SCGTGNLTLN PAHPSFLLPG EPGDIIYDYP EAFNITNATE 

       550        560        570        580        590        600 
AASASAGASS QAAATATTTS TSVSYLRTTP TPGVRNVEHP PYVINHDQEG HDLSVHAVSP 

       610        620        630        640        650        660 
NATHVDGVEE YDVHGLYGHQ GLNATYQGLL EVWSHKRRPF IIGRSTFAGS GKWAGHWGGD 

       670        680        690        700        710        720 
NYSKWWSMYY SISQALSFSL FGIPMFGADT CGFNGNSDEE LCNRWMQLSA FFPFYRNHNE 

       730        740        750        760        770        780 
LSTIPQEPYR WASVIEATKS AMRIRYAILP YFYTLFDLAH TTGSTVMRAL SWEFPNDPTL 

       790        800        810        820        830        840 
AAVETQFMVG PAIMVVPVLE PLVNTVKGVF PGVGHGEVWY DWYTQAAVDA KPGVNTTISA 

       850        860        870        880        890        900 
PLGHIPVYVR GGNILPMQEP ALTTREARQT PWALLAALGS NGTASGQLYL DDGESIYPNA 

       910        920        930        940        950        960 
TLHVDFTASR SSLRSSAQGR WKERNPLANV TVLGVNKEPS AVTLNGQAVF PGSVTYNSTS 

       970        980 
QVLFVGGLQN LTKGGAWAEN WVLEW 

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References

[1]"Cloning and sequencing of an alpha-glucosidase gene from Aspergillus niger and its expression in A. nidulans."
Nakamura A., Nishimura I., Yokoyama A., Lee D.-G., Hidaka M., Masaki H., Kimura A., Chiba S., Uozumi T.
J. Biotechnol. 53:75-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GN-3.
[2]"Complete amino acid sequence of crystalline alpha-glucosidase from Aspergillus niger."
Kimura A., Takata M., Sakai O., Matsui H., Takai N., Takayanagi T., Nishimua I., Uozumi T., Chiba S.
Biosci. Biotechnol. Biochem. 56:1368-1370(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-252 AND 267-985, GLYCOSYLATION AT THR-36; ASN-124; ASN-143; ASN-218; ASN-347; ASN-422; ASN-506; ASN-534; SER-545; SER-550; THR-559; SER-560; THR-561; SER-562; THR-571; ASN-601; ASN-623; ASN-835; ASN-881; SER-895; ASN-899; ASN-957 AND ASN-970.
Strain: GN-8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D45356 Genomic DNA. Translation: BAA23616.1.
PIRJC1199.
JC1200.
JC5561.

3D structure databases

ProteinModelPortalP56526.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00004308.

Chemistry

ChEMBLCHEMBL3435.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.
mycoCLAPAGL31A_ASPNG.

PTM databases

UniCarbKBP56526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1501.

Family and domain databases

InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 2 hits.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGLU_ASPNG
AccessionPrimary (citable) accession number: P56526
Secondary accession number(s): O13451
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: December 11, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries