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Q7Z9L3

- EXGA_ASPOR

UniProt

Q7Z9L3 - EXGA_ASPOR

Protein

Glucan 1,3-beta-glucosidase A

Gene

exgA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase By similarity.By similarity

    Catalytic activityi

    Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

    Cofactori

    Manganese.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei199 – 1991Proton donorBy similarity
    Active sitei298 – 2981NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: ASPGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: ASPGD
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16494.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEXG5A_ASPOR.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase A (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase 1
    Exo-1,3-beta-glucanase A
    Gene namesi
    Name:exgA
    Synonyms:exg1
    ORF Names:AO090003000990
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 2

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Sequence AnalysisAdd
    BLAST
    Chaini15 – 405391Glucan 1,3-beta-glucosidase APRO_0000007876Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi280 ↔ 405By similarity
    Disulfide bondi306 ↔ 332By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    The combination of poor nutrition conditions and attachment of mycelia to a hydrophobic solid surface appears to be a major inducing factor.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ7Z9L3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    OrthoDBiEOG7JT75H.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q7Z9L3-1 [UniParc]FASTAAdd to Basket

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    MLPLLLCIVP YCWSSRLDPR ASSFDYNGEK VRGVNLGGWL VLEPWITPSI    50
    FDAAGAEAVD EWSLTKILGK EEAEARLSAH WKSFVSAGDF QRMADAGLNH 100
    VRIPIGYWAL GPLEGDPYVD GQLEYLDKAV EWAGAAGLKV LIDLHGAPGS 150
    QNGFDNSGRR GAIQWQQGDT VEQTLDAFDL LAERYLGSDT VAAIEAINEP 200
    NIPGGVDQGK LQEYYGSVYG IVNKYNAGTS VVYGDGFLPV ESWNGFKTEG 250
    SKVVMDTHHY HMFDNGLIAM DIDSHIDAVC QFAHQHLEAS DKPVIVGEWT 300
    GAVTDCAKYL NGKGNGARYD GSYAADKAIG DCSSLATGFV SKLSDEERSD 350
    MRRFIEAQLD AFELKSGWVF WTWKTEGAPG WDMSDLLEAG VFPTSPDDRE 400
    FPKQC 405
    Length:405
    Mass (Da):44,373
    Last modified:October 1, 2003 - v1
    Checksum:iFC8D181C0A37A7C9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ566365 Genomic DNA. Translation: CAD97460.1.
    AP007155 Genomic DNA. Translation: BAE58099.1.

    Genome annotation databases

    EnsemblFungiiCADAORAT00001553; CADAORAP00001533; CADAORAG00001553.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ566365 Genomic DNA. Translation: CAD97460.1 .
    AP007155 Genomic DNA. Translation: BAE58099.1 .

    3D structure databases

    ProteinModelPortali Q7Z9L3.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EXG5A_ASPOR.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00001553 ; CADAORAP00001533 ; CADAORAG00001553 .

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    OrthoDBi EOG7JT75H.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16494.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "High glucose-tolerant beta-glucosidase gene from Aspergillus oryzae."
      Riou C., Gunata Z.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. "Purification, characterization, and substrate specificity of a novel highly glucose-tolerant beta-glucosidase from Aspergillus oryzae."
      Riou C., Salmon J.-M., Vallier M.-J., Guenata Z., Barre P.
      Appl. Environ. Microbiol. 64:3607-3614(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
      Strain: ATCC 11489 / CBS 125.59 / IMI 52143 / NRRL 695.
    4. "The beta-1,3-exoglucanase gene exgA (exg1) of Aspergillus oryzae is required to catabolize extracellular glucan, and is induced in growth on a solid surface."
      Tamano K., Satoh Y., Ishii T., Terabayashi Y., Ohtaki S., Sano M., Takahashi T., Koyama Y., Mizutani O., Abe K., Machida M.
      Biosci. Biotechnol. Biochem. 71:926-934(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.

    Entry informationi

    Entry nameiEXGA_ASPOR
    AccessioniPrimary (citable) accession number: Q7Z9L3
    Secondary accession number(s): Q2UK16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 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