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A1C499

- BTGE_ASPCL

UniProt

A1C499 - BTGE_ASPCL

Protein

Probable beta-glucosidase btgE

Gene

btgE

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
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 (23 Jan 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 sitei501 – 5011NucleophileBy similarity
    Active sitei555 – 5551Proton 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:ACLA_059020
    OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
    Taxonomic identifieri344612 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006701: Unassembled WGS sequence

    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 – 564546Probable beta-glucosidase btgEPRO_0000395130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5057.CADACLAP00005509.

    Structurei

    3D structure databases

    ProteinModelPortaliA1C499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.

    A1C499-1 [UniParc]FASTAAdd to Basket

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    MRGAFLATAA AIAGTAMADI AHMRRHGHDS FHQRRAVEQP APEADATCGC    50
    TTEVVTSWGP PTLIPIATSS PSSTVTSEVV TTLHSTSYST VTLVVTPSGA 100
    SPNRESAPAT PAVTLPTPGV TSFSTTGTYT IPATTLTVTH STTVCGATTT 150
    ELPSGTHTYG GVTTVVDRHT TVVCPYATVE PSGSTVTSVI RTTTYVCPSA 200
    GTYTIAPTTT YVPTSTVIVY PTPATITPGT YTQPAQTITV TRDNYIYVCP 250
    FTGQQLPTTA PVAPATTAVP ATTTAVPATT TAVPATSSVA PSSSPSKPAA 300
    PSGAVSGQMG MTYSPYTNEG GCKDKASIIS EVALLKSKGF THVRVYSTDC 350
    GSLEFIGEAA RTSGLRMIIG VFIKQSGVAG AQDQVTAISK WAQWDLVSLI 400
    VVGNESIQNH FCDASTLAGF IVSAKQSFKA AGYSGQVTTT EPINVWQANG 450
    DALCGAVDII GANIHPFFNA DVSAAEAGKF VAQEFKTLKG ICPGKDVINL 500
    ETGWPHSGEA NGKAIPSREE QAIAIKAIAD EVGSMSVFFS YFDDLWKQPG 550
    AFGVERYWGC IENF 564
    Length:564
    Mass (Da):58,575
    Last modified:January 23, 2007 - v1
    Checksum:iB95D30B0D0B75AF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS026990 Genomic DNA. Translation: EAW15239.1.
    RefSeqiXP_001276665.1. XM_001276664.1.

    Genome annotation databases

    EnsemblFungiiCADACLAT00005634; CADACLAP00005509; CADACLAG00005634.
    GeneIDi4708849.
    KEGGiact:ACLA_059020.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS026990 Genomic DNA. Translation: EAW15239.1 .
    RefSeqi XP_001276665.1. XM_001276664.1.

    3D structure databases

    ProteinModelPortali A1C499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5057.CADACLAP00005509.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADACLAT00005634 ; CADACLAP00005509 ; CADACLAG00005634 .
    GeneIDi 4708849.
    KEGGi act:ACLA_059020.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

    Entry informationi

    Entry nameiBTGE_ASPCL
    AccessioniPrimary (citable) accession number: A1C499
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: January 23, 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