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A5ABF5

- BGLM_ASPNC

UniProt

A5ABF5 - BGLM_ASPNC

Protein

Probable beta-glucosidase M

Gene

bglM

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      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 sitei286 – 2861By 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

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable beta-glucosidase M (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase M
    Cellobiase M
    Gentiobiase M
    Gene namesi
    Name:bglM
    ORF Names:An11g00200
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 7R

    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 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 765746Probable beta-glucosidase MPRO_5000242398Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi647 – 6471N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliA5ABF5.
    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.

    A5ABF5-1 [UniParc]FASTAAdd to Basket

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    MHSISALLSL LGGLALSSAA PTQNITSDAY FYGQSPAVYP SPEGTGTGSW    50
    ASAYEKAKAF VAQLTDDEKV NLTAGVSSKT GCSGFIAEIP RLNFTGLCVS 100
    DASNGLRGTD YVNGWSSGIH VGASWNRTLA RDRAKYMGQE FHRKGVNLLL 150
    GPVVGPLGRV AEGGRNWEGF SNDPYLTGAL VYETVQGVQS SGVGVSTKHY 200
    IGNEQETNRN PETVNGVDVA SVSSNIDDKT IHELYLWPFQ DAVLAGSVAI 250
    MCSYERINNS YACQNSKTLN GLLKTELGFQ GYVITDWGAQ HGGIASANAG 300
    LDMVMPETTL WGSNLTTAIA NGTMEASRLD DMATRIIATW YQLNQDTDFP 350
    TPGVGMPASA QSEHQVVVGT APDEKSTLLE SAIEGHVLVK NTNNALPLQT 400
    PQLVSVFGYD AKVTDSFDLA STVLGTSPLF QNYTLWVGGG SGSNSPAYVI 450
    APLNAIQQQA YEDGTSVLWD VSAQDPEVDP TSEACLVFIN SFATEGYDRS 500
    ALTDDYSDTL VTNVASKCNN TIVVVHNAGI RLVYNWIDHE NVTAVVLAHL 550
    PGQDTGHALV DILYGRANPS GKLPYTIAKQ ASDYGSLLHP SEPQTPYGLF 600
    PQSDFSEGVY IDYRAFDKDN ITPQFEFGFG LSYTTFAYSG LSIEKTNETT 650
    SEYPPSAAIQ EGGNPRLWDD LVTVTAEVQN SGSVDGAEVA QLYVGIPNGP 700
    VRQLRGFDKV LLSAGETAQV SFSLNRRDLS TWNVEAQQWQ LQSGTYQVYV 750
    GRSSRDLPLT GEFSI 765
    Length:765
    Mass (Da):82,116
    Last modified:June 12, 2007 - v1
    Checksum:i4D423F77A47A34A1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270218 Genomic DNA. Translation: CAK48253.1.
    RefSeqiXP_001394024.1. XM_001393987.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00008353; CADANGAP00008206; CADANGAG00008353.
    GeneIDi4984238.
    KEGGiang:ANI_1_24094.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270218 Genomic DNA. Translation: CAK48253.1 .
    RefSeqi XP_001394024.1. XM_001393987.1.

    3D structure databases

    ProteinModelPortali A5ABF5.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00008353 ; CADANGAP00008206 ; CADANGAG00008353 .
    GeneIDi 4984238.
    KEGGi ang:ANI_1_24094.

    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. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiBGLM_ASPNC
    AccessioniPrimary (citable) accession number: A5ABF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 36 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