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Q12558 (AGLU_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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
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
Short name=AGL
EC=3.2.1.20
Alternative name(s):
Maltase
Gene names
Name:agdA
ORF Names:AO090003001209
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

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

Induction

By maltose.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 985960Alpha-glucosidase
PRO_0000018577

Sites

Active site4921Nucleophile By similarity
Active site4951 By similarity
Active site6601Proton donor By similarity

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation5391N-linked (GlcNAc...) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Glycosylation6241N-linked (GlcNAc...) Potential
Glycosylation6611N-linked (GlcNAc...) Potential
Glycosylation8351N-linked (GlcNAc...) Potential
Glycosylation8811N-linked (GlcNAc...) Potential
Glycosylation9291N-linked (GlcNAc...) Potential
Glycosylation9571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q12558 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3E9EAE0A0E38209E

FASTA985108,704
        10         20         30         40         50         60 
MAGLKSFLAS SWLLPVACGA SQSIVPSTSA TAAYSQFTIP ASADVGANLV ANIDDPQAVN 

        70         80         90        100        110        120 
AQSVCPGYKA SDVKHSSQGF TASLELAGDP CNVYGTDVDS LTLTVEYQAK DRLNIQIVPT 

       130        140        150        160        170        180 
YFDASNASWY ILSEELVPRP KASQNASVPQ SDFVVSWSNE PSFNFKVIRK ATGDVLFNTK 

       190        200        210        220        230        240 
GSTLVYENQF IEFVTLLPEE YNLYGLGERM NQLRLLENAN LTLYAADIAD PIDDNIYGHH 

       250        260        270        280        290        300 
AFYLDTRYYK VGGQNKSHTI VKSSEAEPSQ EYVSYSHGVF LRNAHGQEIL LRDQKLIWRT 

       310        320        330        340        350        360 
LGGSVDLTFY SGPTQAEVTK QYQLSTVGLP AMQQYNTLGF HQCRWGYNNW SEFEDVLANF 

       370        380        390        400        410        420 
ERFEIPLEYL WADIDYMHGY RNFDNDQHRF SYEEGEKFLN KLHAGGRRWV PIVDGALYIP 

       430        440        450        460        470        480 
NPENASDAYE TYDRGAKDDV FIKNPDGSLY IGAVWPGYTV YPDWHHPKAS DFWANELVTW 

       490        500        510        520        530        540 
WNKLHYDGVW YDMAEVSSFC VGSCGTGNLS MNPAHPPFAL PGEPGNVVYD YPEGFNITNA 

       550        560        570        580        590        600 
TEAASASAGA ASQSAAASST TTSAPYLRTT PTPGVRNVDH PPYVINHVQP GHDLSVHAIS 

       610        620        630        640        650        660 
PNSTHSDGVQ EYDVHSLYGH QGINATYHGL LKVWENKRPF IIARSTFSGS GKWAGHWGGD 

       670        680        690        700        710        720 
NFSKWGSMFF SISQALQFSL FGIPMFGVDT CGFNGNTDEE LCNRWMQLSA FFPFYRNHNV 

       730        740        750        760        770        780 
LSAIPQEPYR WASVIDATKA AMNIRYAILP YFYTLFHLAH TTGSTVMRAL AWEFPNDPSL 

       790        800        810        820        830        840 
AAVGTQFLVG PSVMVIPVLE PQVDTVQGVF PGVGHGEVWY DWYSQTAVDA KPGVNTTISA 

       850        860        870        880        890        900 
PLGHIPVFVR GGSILPMQEV ALTTRDARKT PWSLLASLSS NGTASGQLYL DDGESVYPED 

       910        920        930        940        950        960 
TLSVDFLASR STLRASARGT WKEANPLANV TVLGVTEKPS SVTLNGETLS SDSVKYNATS 

       970        980 
HVLHVGGLQK HTADGAWAKD WVLKW

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and expression of alpha-glucosidase-encoding gene (agdA) from Aspergillus oryzae."
Minetoki T., Gomi K., Kitamoto K., Kumagai C., Tamura G.
Biosci. Biotechnol. Biochem. 59:1516-1521(1995) [PubMed: 7549103] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.
[2]"Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae."
Gomi K., Akeno T., Minetoki T., Ozeki K., Kumagai C., Okazaki N., Iimura Y.
Biosci. Biotechnol. Biochem. 64:816-827(2000) [PubMed: 10830498] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.
[3]"Genome sequencing and analysis of Aspergillus oryzae."
Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. expand/collapse author list , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D45179 Genomic DNA. Translation: BAA08125.1.
AB021876 Genomic DNA. Translation: BAA95702.1.
AP007155 Genomic DNA. Translation: BAE58289.1.
PIRJC4217.
RefSeqXP_001820291.1. XM_001820239.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ12558.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00001748; CADAORAP00001723; CADAORAG00001748.
GeneID5992274.
GenomeReviewsGene locus agdA in contig AP007155_GR.
KEGGaor:AOR_1_2146154.

Phylogenomic databases

GeneTreeEFGT00050000002321.
OrthoDBEOG4J40R4.

Family and domain databases

InterProIPR011013. Glyco_hydro-type_carb-bd.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
KOK01187.
PANTHERPTHR22762. Glyco_hydro_31. 1 hit.
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF74650. Gal_mut_like. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGLU_ASPOR
AccessionPrimary (citable) accession number: Q12558
Secondary accession number(s): Q7LWA9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents