Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P36914 (AMYG_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. 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:
Glucoamylase

EC=3.2.1.3
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene names
Name:glaA
Synonyms:gluB
ORF Names:AO090010000746
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Sequence similarities

Belongs to the glycosyl hydrolase 15 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 256 By similarity
PRO_0000001465
Chain26 – 612587Glucoamylase
PRO_0000001466

Regions

Domain506 – 612107CBM20

Sites

Active site2021Proton acceptor By similarity
Active site2051Proton donor By similarity
Binding site1461Substrate By similarity

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential
Disulfide bond236 ↔ 239 By similarity
Disulfide bond248 ↔ 475 By similarity
Disulfide bond288 ↔ 296 By similarity

Experimental info

Sequence conflict1721G → S in BAA00841. Ref.1
Sequence conflict1721G → S in BAA01540. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P36914 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 7C36E1B0A341CEDA

FASTA61265,457
        10         20         30         40         50         60 
MVSFSSCLRA LALGSSVLAV QPVLRQATGL DTWLSTEANF SRQAILNNIG ADGQSAQGAS 

        70         80         90        100        110        120 
PGVVIASPSK SDPDYFYTWT RDSGLVMKTL VDLFRGGDAD LLPIIEEFIS SQARIQGISN 

       130        140        150        160        170        180 
PSGALSSGGL GEPKFNVDET AFTGAWGRPQ RDGPALRATA MISFGEWLVE NGHTSIATDL 

       190        200        210        220        230        240 
VWPVVRNDLS YVAQYWSQSG FDLWEEVQGT SFFTVAVSHR ALVEGSSFAK TVGSSCPYCD 

       250        260        270        280        290        300 
SQAPQVRCYL QSFWTGSYIQ ANFGGGRSGK DINTVLGSIH TFDPQATCDD ATFQPCSARA 

       310        320        330        340        350        360 
LANHKVVTDS FRSIYAINSG RAENQAVAVG RYPEDSYYNG NPWFLTTLAA AEQLYDALYQ 

       370        380        390        400        410        420 
WDKIGSLAIT DVSLPFFKAL YSSAATGTYA SSTTVYKDIV SAVKAYADGY VQIVQTYAAS 

       430        440        450        460        470        480 
TGSMAEQYTK TDGSQTSARD LTWSYAALLT ANNRRNAVVP APWGETAATS IPSACSTTSA 

       490        500        510        520        530        540 
SGTYSSVVIT SWPTISGYPG APDSPCQVPT TVSVTFAVKA TTVYGESIKI VGSISQLGSW 

       550        560        570        580        590        600 
NPSSATALNA DSYTTDNPLW TGTINLPAGQ SFEYKFIRVQ NGAVTWESDP NRKYTVPSTC 

       610 
GVKSAVQSDV WR 

« Hide

References

« Hide 'large scale' references
[1]"The glucoamylase cDNA from Aspergillus oryzae: its cloning, nucleotide sequence, and expression in Saccharomyces cerevisiae."
Hata Y., Kitamoto K., Gomi K., Kumagai C., Tamura G., Hara S.
Agric. Biol. Chem. 55:941-949(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence and expression of the glucoamylase-encoding gene (glaA) from Aspergillus oryzae."
Hata Y., Tsuchiya K., Kitamoto K., Gomi K., Kumagai C., Tamura G., Hara S.
Gene 108:145-150(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.
[3]Ma L., Chen D., Chen X., Wang H.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D01035 mRNA. Translation: BAA00841.1.
D10698 Genomic DNA. Translation: BAA01540.1.
DQ211971 mRNA. Translation: ABA62323.1.
AP007175 Genomic DNA. Translation: BAE66563.1.
PIRJQ1346.
RefSeqXP_001827696.1. XM_001827644.2.

3D structure databases

ProteinModelPortalP36914.
SMRP36914. Positions 30-612.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00004691.

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPGLA15A_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00004778; CADAORAP00004691; CADAORAG00004778.
GeneID5999830.
KEGGaor:AOR_1_1262024.

Phylogenomic databases

eggNOGCOG3387.
HOGENOMHOG000182646.
KOK01178.
OMANGNPWFL.
OrthoDBEOG7NPG4B.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSPR00736. GLHYDRLASE15.
SMARTSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYG_ASPOR
AccessionPrimary (citable) accession number: P36914
Secondary accession number(s): Q3HLW7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 2, 2006
Last modified: June 11, 2014
This is version 99 of the entry and version 2 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