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B0XN12

- EXGA_ASPFC

UniProt

B0XN12 - EXGA_ASPFC

Protein

Probable glucan 1,3-beta-glucosidase A

Gene

exgA

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
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    Functioni

    Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase By similarity.By similarity

    Catalytic activityi

    Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

    Cofactori

    Manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei211 – 2111Proton donorBy similarity
    Active sitei308 – 3081NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glucan 1,3-beta-glucosidase A (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase 1
    Exo-1,3-beta-glucanase A
    Gene namesi
    Name:exgA
    Synonyms:exg1
    ORF Names:AFUB_004010
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: Unassembled WGS sequence

    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 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 416394Probable glucan 1,3-beta-glucosidase APRO_0000393528Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi291 ↔ 415By similarity
    Disulfide bondi316 ↔ 342By similarity
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliB0XN12.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000114462.
    OrthoDBiEOG7JT75H.
    PhylomeDBiB0XN12.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    B0XN12-1 [UniParc]FASTAAdd to Basket

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    MIFKFSQKAL VALYLVVGLA EAVPSKSRVV SRASTFDYNG IVRGVNIGGW    50
    LVLEPWITPS IFDNAGDAAV DEWTLTATLG QDQAKAVLSQ HWSTFITQDD 100
    FQQIAQAGMN HVRIPIGYWA VSSLPDEPYV DGQLEYLDNA ISWAREAGLK 150
    VVIDLHGAPG SQNGFDNSGR KGPIAWQQGD TVSQTVDAFR ALAERYLPQS 200
    DVVTAIEALN EPNIPGGVSE AGLRDYYNQI ADVVRQIDPD TSVFLSDGFL 250
    STESWNGFKT GEDVVMDTHH YEMFDNYLIS LDIDGHVKSA CDFGKQIEGS 300
    DKPVVVGEWS GAVTDCTKHL NGKGVSTRYQ GEYANNVKYG DCANTTQGSV 350
    ADLSDQERTD TRRFIEAQLD AYEGKNGWLF WTWKTEGAPG WDMQDLLANG 400
    VFPSPLTDRQ FPNQCA 416
    Length:416
    Mass (Da):45,745
    Last modified:April 8, 2008 - v1
    Checksum:iB55EB08627F6F28D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499594 Genomic DNA. Translation: EDP55704.1.

    Genome annotation databases

    EnsemblFungiiCADAFUBT00000402; CADAFUBP00000394; CADAFUBG00000402.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499594 Genomic DNA. Translation: EDP55704.1 .

    3D structure databases

    ProteinModelPortali B0XN12.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUBT00000402 ; CADAFUBP00000394 ; CADAFUBG00000402 .

    Phylogenomic databases

    HOGENOMi HOG000114462.
    OrthoDBi EOG7JT75H.
    PhylomeDBi B0XN12.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CEA10 / CBS 144.89 / FGSC A1163.

    Entry informationi

    Entry nameiEXGA_ASPFC
    AccessioniPrimary (citable) accession number: B0XN12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 35 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3