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Q5BD29

- BTGE_EMENI

UniProt

Q5BD29 - BTGE_EMENI

Protein

Probable beta-glucosidase btgE

Gene

btgE

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      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 sitei488 – 4881NucleophileBy similarity
    Active sitei546 – 5461Proton 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.

    Protein family/group databases

    CAZyiGH17. Glycoside Hydrolase Family 17.

    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:AN1551
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VII

    Subcellular locationi

    Secretedcell wall 1 Publication
    Note: Covalently-linked to the cell wall.

    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 – 555537Probable beta-glucosidase btgEPRO_0000395136Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ5BD29.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi49 – 288240Thr-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.

    Q5BD29-1 [UniParc]FASTAAdd to Basket

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    MRGAILATAA AFAGTAVADM HMRRHAHEGL HHRALHASSA VPEEECGCTT    50
    EVITYWGEPT TIPLSVPTST VTSETTETVH STSYSTVTVT ATSSAAPVET 100
    PSETPSPTPE VTLPTAGVTS YSETGTYTIP ATTITVTDTT TVCGATTTEL 150
    PSGTHTYGGV TTIVETATTI TCPYATVKPT GSTVTSVIET TTYVCPSAGT 200
    YTIAPTTTFV PTSTVVVYPT PETVTPGTYT NPGTTITVTR TEDVYVCPYT 250
    NGNVPTSVPA LPTTSAASTT TAVPSSSTTT SSATSVPTGA SGNKMGMTFT 300
    PYNNDGSCMA KNDVLEQVGL IKGKGFSHVR VYGTDCHTLE YVGAACSTHG 350
    LKMILGVNVE GSTGFDGARS QFKDITNWGQ WDLVSLIVVG NEVVTSNIAS 400
    AAQLASFVSE GASAFSAAGY TGQVTTAEPI DVWLSNGATL CPVVDILGAN 450
    LHPFFNPEFT AAEAGTLVSN QIKDLKQVCT GKDVINLETG WPNAGSANGK 500
    AIPGQSQQTT AIKSLVEKVG DVSVFFSYAD DGWKSKFATS DKYNVEQHWG 550
    CIDQF 555
    Length:555
    Mass (Da):57,672
    Last modified:April 26, 2005 - v1
    Checksum:iB8F0DF0153079DCA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490473 mRNA. Translation: ABF50849.1.
    AACD01000025 Genomic DNA. Translation: EAA64258.1.
    BN001307 Genomic DNA. Translation: CBF85093.1.
    RefSeqiXP_659155.1. XM_654063.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00008179; CADANIAP00008179; CADANIAG00008179.
    GeneIDi2874885.
    KEGGiani:AN1551.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490473 mRNA. Translation: ABF50849.1 .
    AACD01000025 Genomic DNA. Translation: EAA64258.1 .
    BN001307 Genomic DNA. Translation: CBF85093.1 .
    RefSeqi XP_659155.1. XM_654063.1.

    3D structure databases

    ProteinModelPortali Q5BD29.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH17. Glycoside Hydrolase Family 17.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00008179 ; CADANIAP00008179 ; CADANIAG00008179 .
    GeneIDi 2874885.
    KEGGi ani:AN1551.2.

    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. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
      Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "Comprehensive genomic analysis of cell wall genes in Aspergillus nidulans."
      de Groot P.W., Brandt B.W., Horiuchi H., Ram A.F., de Koster C.G., Klis F.M.
      Fungal Genet. Biol. 46:S72-S81(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiBTGE_EMENI
    AccessioniPrimary (citable) accession number: Q5BD29
    Secondary accession number(s): C8VMY9, Q1HFV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 58 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