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Q2US39

- BTGE_ASPOR

UniProt

Q2US39 - BTGE_ASPOR

Protein

Probable beta-glucosidase btgE

Gene

btgE

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.By similarity

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei538 – 5381NucleophileBy similarity
    Active sitei592 – 5921Proton donorBy similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00696.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable beta-glucosidase btgE (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase btgE
    Cellobiase btgE
    Gentiobiase btgE
    Gene namesi
    Name:btgE
    ORF Names:AO090005000582
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 1

    Subcellular locationi

    Secretedcell wall By similarity
    Note: Covalently-linked to the cell wall.By similarity

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell wall, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 602584Probable beta-glucosidase btgEPRO_0000395134Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5062.CADAORAP00002524.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2US39.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi94 – 321228Thr-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5309.
    HOGENOMiHOG000158427.
    OMAiYSTDCDT.
    OrthoDBiEOG73FQWG.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q2US39-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRGAFLAAAA AVAGTAMADV AHMRRHGHDS FHHNRAYQPE VPAEGDENCE    50
    CTTKVITITG PPTLVPINTP APEPSSSSSS EVPSVPSSES SVVTSEAVTT 100
    LHSTSTATVT VVTTPGVDAT GAQTPTGGVP GTPEASSPAG TPEASTPAVP 150
    ATSESPLPTP GVTSFSSTGI YTIPATTVTV RDTTTVCGAT TTELPSGTHT 200
    FGGVTTVVST ATTVTCPVAT VEPSGSTVTS KIYTTTYVCP SAGTYTIAPT 250
    TTYVPTSTVV VYPTPATITP GTYTQDEQTV TVTRTDFTYV CPFTGNDQPT 300
    SAPVASTSAV PVTTTAAPST TSAVASSSAS ASSTATAVPT GVSGQQMGMT 350
    YSPYTNEGGC QSKDQVLKDV ALIKQKGFTH VRVYSTDCNG LEYIGEAARE 400
    NGLKMIIGVF ISSTGISGAQ EQVTAITKWA QWDLVTLVVV GNEAIQNGYT 450
    DASSLAGFIS SCKSSFQASG YSGQVTTTEP INVWQQSGSA LCGAVDILGA 500
    NLHPFFNADV TPDQAGSFVR AQIKDLEAVC NKDVINLETG WPSAGNANGK 550
    AVPGTAQQAA AIKALVEEVG SQSVFFSYSN DLWKDAGEFD VERYWGCIDQ 600
    FK 602
    Length:602
    Mass (Da):61,824
    Last modified:January 24, 2006 - v1
    Checksum:i94BCCF3A057E95D7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007151 Genomic DNA. Translation: BAE55626.1.

    Genome annotation databases

    EnsemblFungiiCADAORAT00002562; CADAORAP00002524; CADAORAG00002562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007151 Genomic DNA. Translation: BAE55626.1 .

    3D structure databases

    ProteinModelPortali Q2US39.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5062.CADAORAP00002524.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00002562 ; CADAORAP00002524 ; CADAORAG00002562 .

    Phylogenomic databases

    eggNOGi COG5309.
    HOGENOMi HOG000158427.
    OMAi YSTDCDT.
    OrthoDBi EOG73FQWG.

    Enzyme and pathway databases

    UniPathwayi UPA00696 .

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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 nameiBTGE_ASPOR
    AccessioniPrimary (citable) accession number: Q2US39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 48 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3