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A1DBG6

- BTGE_NEOFI

UniProt

A1DBG6 - BTGE_NEOFI

Protein

Probable beta-glucosidase btgE

Gene

btgE

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (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 sitei488 – 4881NucleophileBy similarity
    Active sitei542 – 5421Proton 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:NFIA_098360
    OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
    Taxonomic identifieri331117 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
    ProteomesiUP000006702: 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 – 552534Probable beta-glucosidase btgEPRO_0000395137Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi36630.CADNFIAP00009054.

    Structurei

    3D structure databases

    ProteinModelPortaliA1DBG6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi44 – 268225Thr-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5309.
    HOGENOMiHOG000158427.
    OMAiSAMSSHQ.
    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.

    A1DBG6-1 [UniParc]FASTAAdd to Basket

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    MRGAILATAA ALAGTAMADV AHMRRHGHDS FHQRRAAVAE ADATCGCTTE    50
    VVTVWGPPTL IPVATPTPST VTSEAVTTLH STSTSTVTIV ASASTPATSS 100
    SPATPKVPLP TPAITNFPST GVYTIPATTV TVFDTTTVCG ATTTELPAGT 150
    HTYGGVTTVV ETATTVVCPY ATVEPSGTTV TSVIKTTTYV CPTPGTYTIA 200
    PTTTTVPTST VVVYPTPAVI TPGTYTQPEQ TVTVTRTDYT YVCPFTGQNE 250
    PTSAPAAPST TAVPATTTAA VPSTSSAAPS SSSTAPASTG AVGGQMGMTY 300
    TPYTKGGDCK DKSSVLSEVA NLKSKGFTHV RVYSTDCNSL EYIGEAARTS 350
    GLQMIIGVFI SSTGVSGAQD QVTAISKWAQ WDLVSLIVVG NEAIQNGYCD 400
    ASTLAGFISS AKSAFQSAGY TGKVTTTEPI NVWQAYGSTL CGVCDIIGAN 450
    IHPFFNADVS ADQAGKFVAQ EIKVLEGICP GKDVLNLETG WPHAGNANGK 500
    AVPGASEQAI AIKSIAQEVG SKSVFFSYFD DLWKEPGQFD VERYWGCIDT 550
    FN 552
    Length:552
    Mass (Da):56,907
    Last modified:January 23, 2007 - v1
    Checksum:iC8E05DAC3193C2A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027694 Genomic DNA. Translation: EAW20206.1.
    RefSeqiXP_001262103.1. XM_001262102.1.

    Genome annotation databases

    EnsemblFungiiCADNFIAT00009268; CADNFIAP00009054; CADNFIAG00009268.
    GeneIDi4588449.
    KEGGinfi:NFIA_098360.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027694 Genomic DNA. Translation: EAW20206.1 .
    RefSeqi XP_001262103.1. XM_001262102.1.

    3D structure databases

    ProteinModelPortali A1DBG6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 36630.CADNFIAP00009054.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADNFIAT00009268 ; CADNFIAP00009054 ; CADNFIAG00009268 .
    GeneIDi 4588449.
    KEGGi nfi:NFIA_098360.

    Phylogenomic databases

    eggNOGi COG5309.
    HOGENOMi HOG000158427.
    OMAi SAMSSHQ.
    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 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

    Entry informationi

    Entry nameiBTGE_NEOFI
    AccessioniPrimary (citable) accession number: A1DBG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 38 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

    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