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P36914

- AMYG_ASPOR

UniProt

P36914 - AMYG_ASPOR

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Protein

Glucoamylase

Gene

glaA

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 – 1461SubstrateBy similarity
Active sitei202 – 2021Proton acceptorPROSITE-ProRule annotation
Active sitei205 – 2051Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

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

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 – 1919By similarityAdd
BLAST
Propeptidei20 – 256By similarityPRO_0000001465
Chaini26 – 612587GlucoamylasePRO_0000001466Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00004691.

Structurei

3D structure databases

ProteinModelPortaliP36914.
SMRiP36914. Positions 30-612.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini506 – 612107CBM20PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MVSFSSCLRA LALGSSVLAV QPVLRQATGL DTWLSTEANF SRQAILNNIG
60 70 80 90 100
ADGQSAQGAS PGVVIASPSK SDPDYFYTWT RDSGLVMKTL VDLFRGGDAD
110 120 130 140 150
LLPIIEEFIS SQARIQGISN PSGALSSGGL GEPKFNVDET AFTGAWGRPQ
160 170 180 190 200
RDGPALRATA MISFGEWLVE NGHTSIATDL VWPVVRNDLS YVAQYWSQSG
210 220 230 240 250
FDLWEEVQGT SFFTVAVSHR ALVEGSSFAK TVGSSCPYCD SQAPQVRCYL
260 270 280 290 300
QSFWTGSYIQ ANFGGGRSGK DINTVLGSIH TFDPQATCDD ATFQPCSARA
310 320 330 340 350
LANHKVVTDS FRSIYAINSG RAENQAVAVG RYPEDSYYNG NPWFLTTLAA
360 370 380 390 400
AEQLYDALYQ WDKIGSLAIT DVSLPFFKAL YSSAATGTYA SSTTVYKDIV
410 420 430 440 450
SAVKAYADGY VQIVQTYAAS TGSMAEQYTK TDGSQTSARD LTWSYAALLT
460 470 480 490 500
ANNRRNAVVP APWGETAATS IPSACSTTSA SGTYSSVVIT SWPTISGYPG
510 520 530 540 550
APDSPCQVPT TVSVTFAVKA TTVYGESIKI VGSISQLGSW NPSSATALNA
560 570 580 590 600
DSYTTDNPLW TGTINLPAGQ SFEYKFIRVQ NGAVTWESDP NRKYTVPSTC
610
GVKSAVQSDV WR
Length:612
Mass (Da):65,457
Last modified:May 2, 2006 - v2
Checksum:i7C36E1B0A341CEDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721G → S in BAA00841. (PubMed:1368680)Curated
Sequence conflicti172 – 1721G → S in BAA01540. (PubMed:1761224)Curated

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...
MobiDBi 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: October 1, 2014
This is version 100 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, Reference 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