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A2RAL4

- BGLA_ASPNC

UniProt

A2RAL4 - BGLA_ASPNC

Protein

Probable beta-glucosidase A

Gene

bglA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (06 Mar 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 sitei280 – 2801By similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC
    2. glucosidase activity Source: ASPGD

    GO - Biological processi

    1. cellular carbohydrate catabolic process Source: ASPGD
    2. 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 A (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase A
    Cellobiase A
    Gentiobiase A
    Gene namesi
    Name:bglA
    Synonyms:bgl1
    ORF Names:An18g03570
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 8L

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. intracellular Source: ASPGD

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 860841Probable beta-glucosidase APRO_5000221323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi442 – 4421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi542 – 5421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiA2RAL4.

    Structurei

    3D structure databases

    ProteinModelPortaliA2RAL4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    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.
    IPR019800. Glyco_hydro_3_AS.
    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.
    PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    A2RAL4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRFTSIEAVA LTAVSLASAD ELAYSPPYYP SPWANGQGDW AEAYQRAVDI    50
    VSQMTLAEKV NLTTGTGWEL ELCVGQTGGV PRLGIPGMCA QDSPLGVRDS 100
    DYNSAFPAGV NVAATWDKNL AYLRGQAMGQ EFSDKGADIQ LGPAAGPLGR 150
    SPDGGRNWEG FSPDPALSGV LFAETIKGIQ DAGVVATAKH YIAYEQEHFR 200
    QAPEAQGYGF NITESGSANL DDKTMHELYL WPFADAIRAG AGAVMCSYNQ 250
    INNSYGCQNS YTLNKLLKAE LGFQGFVMSD WAAHHAGVSG ALAGLDMSMP 300
    GDVDYDSGTS YWGTNLTISV LNGTVPQWRV DDMAVRIMAA YYKVGRDRLW 350
    TPPNFSSWTR DEYGFKYYYV SEGPYEKVNQ FVNVQRNHSE LIRRIGADST 400
    VLLKNDGALP LTGKERLVAL IGEDAGSNPY GANGCSDRGC DNGTLAMGWG 450
    SGTANFPYLV TPEQAISNEV LKNKNGVFTA TDNWAIDQIE ALAKTASVSL 500
    VFVNADSGEG YINVDGNLGD RRNLTLWRNG DNVIKAAASN CNNTIVIIHS 550
    VGPVLVNEWY DNPNVTAILW GGLPGQESGN SLADVLYGRV NPGAKSPFTW 600
    GKTREAYQDY LYTEPNNGNG APQEDFVEGV FIDYRGFDKR NETPIYEFGY 650
    GLSYTTFNYS NLQVEVLSAP AYEPASGETE AAPTFGEVGN ASDYLYPDGL 700
    QRITKFIYPW LNSTDLEASS GDASYGQDAS DYLPEGATDG SAQPILPAGG 750
    GAGGNPRLYD ELIRVSVTIK NTGKVAGDEV PQLYVSLGGP NEPKIVLRQF 800
    ERITLQPSKE TQWSTTLTRR DLANWNVETQ DWEITSYPKM VFAGSSSRKL 850
    PLRASLPTVH 860
    Length:860
    Mass (Da):93,229
    Last modified:March 6, 2007 - v1
    Checksum:i087215D2E1F89643
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270402 Genomic DNA. Translation: CAK48740.1.
    RefSeqiXP_001398816.1. XM_001398779.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00013994; CADANGAP00013734; CADANGAG00013994.
    GeneIDi4989921.
    KEGGiang:ANI_1_456164.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270402 Genomic DNA. Translation: CAK48740.1 .
    RefSeqi XP_001398816.1. XM_001398779.2.

    3D structure databases

    ProteinModelPortali A2RAL4.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Proteomic databases

    PRIDEi A2RAL4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00013994 ; CADANGAP00013734 ; CADANGAG00013994 .
    GeneIDi 4989921.
    KEGGi ang:ANI_1_456164.

    Phylogenomic databases

    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.
    IPR019800. Glyco_hydro_3_AS.
    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.
    PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view ]
    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 nameiBGLA_ASPNC
    AccessioniPrimary (citable) accession number: A2RAL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 44 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