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P36914

- AMYG_ASPOR

UniProt

P36914 - AMYG_ASPOR

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
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    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

    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

    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

    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

    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

    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