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Q5B0F4

- BGLG_EMENI

UniProt

Q5B0F4 - BGLG_EMENI

Protein

Probable beta-glucosidase G

Gene

bglG

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      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 sitei305 – 3051By 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 G (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase G
    Cellobiase G
    Gentiobiase G
    Gene namesi
    Name:bglG
    ORF Names:AN5976
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome I

    Subcellular locationi

    Secreted By similarity

    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 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 819799Probable beta-glucosidase GPRO_0000394119Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi500 – 5001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi554 – 5541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi627 – 6271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi683 – 6831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi719 – 7191N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B0F4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1472.
    HOGENOMiHOG000031215.
    KOiK05349.
    OrthoDBiEOG7HMS8F.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProiIPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view]
    PRINTSiPR00133. GLHYDRLASE3.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    Q5B0F4-1 [UniParc]FASTAAdd to Basket

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    MTSASQILVW GLLAASGAQA QNYGGGSSRS DDAFSYVQPK NTTILGAYGH    50
    SPAVYPSPNT TGSGGWETAL AQAQDFVAQL TLEEKANMVT GQPGPCVGNI 100
    IAIPRLNFSG LCLQDGPLAI RVTDMASVFS AGVTAAASWD RKILYERGYA 150
    MGQEFKAKGA HVALGPVAGP LGRSAYSGRN WEGFAADPYL TGVAMEETIQ 200
    GYQDAGVQAC PKHFIGNEQE TMRNPTFNDS APLGTVIQEA VSSNIDDRTM 250
    HELYLWPFAN AVHAKAASIM CSYQRINGSY GCENSKTLNG LLKGELGFQG 300
    YVMSDWGATH SGVAGIKSGQ DMDMPGGLGA YGQTFINRSF FGGNVTAAVN 350
    NGTLEESRID DMILRIMTPY FWLGQDQDYP TVDPSTADYN TFSPRNTWYQ 400
    DFNLTGERSR DVRGNHAALI RKQAAEATVL LKNKNNALPL KAPKTLAVFG 450
    NDASDITNGP YNDATYEYGT LAAGGGSGTG RFTYLVSPLT AINARAQKDN 500
    TSLVQFWLNN TQIATSDVQA DLLRVPTPPT ACLVFVKTWA EEGADREHLR 550
    LDYNGTEVVE AVAAACNNTI VVTHSSGINE LPFANHPNVT AILAAHFPGQ 600
    ESGNSIVDVL YGDVNPSGRL PYTIARNGSD YNAPPTTAVT TSGREDWQSW 650
    FDEKLEIDYR YFDAHNIPVL YEFGFGLSYT TFNISDIYAT RVVDSITSAP 700
    EDRAIQPGGN PELWETIYNV TVSVTNTGDV EGATVPQLYV TFPDSTPEGT 750
    PPKQLRGFDK VSLQPGESTK VIFELMRRDL SYWDTVSQQW LIPEGDFTIR 800
    VGFSSRNLKE VTTITPVSE 819
    Length:819
    Mass (Da):88,639
    Last modified:May 18, 2010 - v2
    Checksum:i932C81818E1B7F6B
    GO

    Sequence cautioni

    The sequence CBF70434.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAA57725.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000102 Genomic DNA. Translation: EAA57725.1. Different initiation.
    BN001301 Genomic DNA. Translation: CBF70434.1. Different initiation.
    RefSeqiXP_663580.1. XM_658488.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00007042; CADANIAP00007042; CADANIAG00007042.
    GeneIDi2870885.
    KEGGiani:AN5976.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACD01000102 Genomic DNA. Translation: EAA57725.1 . Different initiation.
    BN001301 Genomic DNA. Translation: CBF70434.1 . Different initiation.
    RefSeqi XP_663580.1. XM_658488.1.

    3D structure databases

    ProteinModelPortali Q5B0F4.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00007042 ; CADANIAP00007042 ; CADANIAG00007042 .
    GeneIDi 2870885.
    KEGGi ani:AN5976.2.

    Phylogenomic databases

    eggNOGi COG1472.
    HOGENOMi HOG000031215.
    KOi K05349.
    OrthoDBi EOG7HMS8F.

    Enzyme and pathway databases

    UniPathwayi UPA00696 .

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProi IPR026891. Fn3-like.
    IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR30620. PTHR30620. 1 hit.
    Pfami PF14310. Fn3-like. 1 hit.
    PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00133. GLHYDRLASE3.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. "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.

    Entry informationi

    Entry nameiBGLG_EMENI
    AccessioniPrimary (citable) accession number: Q5B0F4
    Secondary accession number(s): C8V3B8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 53 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3