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P36914

- AMYG_ASPOR

UniProt

P36914 - AMYG_ASPOR

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Protein
Glucoamylase
Gene
glaA, gluB, AO090010000746
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei146 – 1461Substrate By similarity
Active sitei202 – 2021Proton acceptor By similarity
Active sitei205 – 2051Proton donor By similarity

GO - Molecular functioni

  1. glucan 1,4-alpha-glucosidase activity Source: ASPGD
  2. starch binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
  2. polysaccharide metabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPiGLA15A_ASPOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:glaA
Synonyms:gluB
ORF Names:AO090010000746
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 8

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: ASPGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarity
Add
BLAST
Propeptidei20 – 256 By similarity
PRO_0000001465
Chaini26 – 612587Glucoamylase
PRO_0000001466Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi236 ↔ 239 By similarity
Disulfide bondi248 ↔ 475 By similarity
Disulfide bondi288 ↔ 296 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00004691.

Structurei

3D structure databases

ProteinModelPortaliP36914.
SMRiP36914. Positions 30-612.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini506 – 612107CBM20
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3387.
HOGENOMiHOG000182646.
KOiK01178.
OMAiNGNPWFL.
OrthoDBiEOG7NPG4B.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 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]
PfamiPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFiPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSiPR00736. GLHYDRLASE15.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P36914-1 [UniParc]FASTAAdd to Basket

« Hide

MVSFSSCLRA LALGSSVLAV QPVLRQATGL DTWLSTEANF SRQAILNNIG    50
ADGQSAQGAS PGVVIASPSK SDPDYFYTWT RDSGLVMKTL VDLFRGGDAD 100
LLPIIEEFIS SQARIQGISN PSGALSSGGL GEPKFNVDET AFTGAWGRPQ 150
RDGPALRATA MISFGEWLVE NGHTSIATDL VWPVVRNDLS YVAQYWSQSG 200
FDLWEEVQGT SFFTVAVSHR ALVEGSSFAK TVGSSCPYCD SQAPQVRCYL 250
QSFWTGSYIQ ANFGGGRSGK DINTVLGSIH TFDPQATCDD ATFQPCSARA 300
LANHKVVTDS FRSIYAINSG RAENQAVAVG RYPEDSYYNG NPWFLTTLAA 350
AEQLYDALYQ WDKIGSLAIT DVSLPFFKAL YSSAATGTYA SSTTVYKDIV 400
SAVKAYADGY VQIVQTYAAS TGSMAEQYTK TDGSQTSARD LTWSYAALLT 450
ANNRRNAVVP APWGETAATS IPSACSTTSA SGTYSSVVIT SWPTISGYPG 500
APDSPCQVPT TVSVTFAVKA TTVYGESIKI VGSISQLGSW NPSSATALNA 550
DSYTTDNPLW TGTINLPAGQ SFEYKFIRVQ NGAVTWESDP NRKYTVPSTC 600
GVKSAVQSDV WR 612
Length:612
Mass (Da):65,457
Last modified:May 2, 2006 - v2
Checksum:i7C36E1B0A341CEDA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721G → S in BAA00841. 1 Publication
Sequence conflicti172 – 1721G → S in BAA01540. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D01035 mRNA. Translation: BAA00841.1.
D10698 Genomic DNA. Translation: BAA01540.1.
DQ211971 mRNA. Translation: ABA62323.1.
AP007175 Genomic DNA. Translation: BAE66563.1.
PIRiJQ1346.
RefSeqiXP_001827696.1. XM_001827644.2.

Genome annotation databases

EnsemblFungiiCADAORAT00004778; CADAORAP00004691; CADAORAG00004778.
GeneIDi5999830.
KEGGiaor:AOR_1_1262024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D01035 mRNA. Translation: BAA00841.1 .
D10698 Genomic DNA. Translation: BAA01540.1 .
DQ211971 mRNA. Translation: ABA62323.1 .
AP007175 Genomic DNA. Translation: BAE66563.1 .
PIRi JQ1346.
RefSeqi XP_001827696.1. XM_001827644.2.

3D structure databases

ProteinModelPortali P36914.
SMRi P36914. Positions 30-612.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00004691.

Protein family/group databases

CAZyi CBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPi GLA15A_ASPOR.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00004778 ; CADAORAP00004691 ; CADAORAG00004778 .
GeneIDi 5999830.
KEGGi aor:AOR_1_1262024.

Phylogenomic databases

eggNOGi COG3387.
HOGENOMi HOG000182646.
KOi K01178.
OMAi NGNPWFL.
OrthoDBi EOG7NPG4B.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProi IPR008928. 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 ]
Pfami PF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view ]
PIRSFi PIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSi PR00736. GLHYDRLASE15.
SMARTi SM01065. CBM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEi PS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAMYG_ASPOR
AccessioniPrimary (citable) accession number: P36914
Secondary accession number(s): Q3HLW7
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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