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A2RAR6

- EXGA_ASPNC

UniProt

A2RAR6 - EXGA_ASPNC

Protein

Probable glucan 1,3-beta-glucosidase A

Gene

exgA

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 45 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      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 sitei210 – 2101Proton 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

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    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:An18g04100
    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

    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_5000221332Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi290 ↔ 415By similarity
    Disulfide bondi316 ↔ 342By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00013786.

    Structurei

    3D structure databases

    ProteinModelPortaliA2RAR6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    KOiK01210.
    OrthoDBiEOG7JT75H.

    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.

    A2RAR6-1 [UniParc]FASTAAdd to Basket

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    MFVESAKKAL LALSLLAASA QAVPRVRRQG ASSSFDYKSQ IVRGVNLGGW    50
    LVTEPWITPS LYDSTGGGAV DEWTLCQILG KDEAQAKLSS HWSSFITQSD 100
    FDRMAQAGLN HVRIPIGYWA VAPIDGEPYV SGQIDYLDQA VTWARAAGLK 150
    VLVDLHGAPG SQNGFDNSGH RGPIQWQQGD TVNQTMTAFD ALARRYAQSD 200
    TVTAIEAVNE PNIPGGVNED GLKNYYYGAL ADVQRLNPST TLFMSDGFQP 250
    VESWNGFMQG SNVVMDTHHY QVFDTGLLSM SIDDHVKTAC SLATQHTMQS 300
    DKPVVVGEWT GALTDCAKYL NGVGNAARYD GTYMSTTKYG DCTGKSTGSV 350
    ADFSADEKAN TRRYIEAQLE AYEMKSGWLF WTWKTEGAPG WDMQDLLANQ 400
    LFPTSPTDRQ YPHQCS 416
    Length:416
    Mass (Da):45,526
    Last modified:March 6, 2007 - v1
    Checksum:i9FC5AADB23A03E24
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270406 Genomic DNA. Translation: CAK43212.1.
    RefSeqiXP_001398868.1. XM_001398831.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00014047; CADANGAP00013786; CADANGAG00014047.
    GeneIDi4989974.
    KEGGiang:ANI_1_534164.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270406 Genomic DNA. Translation: CAK43212.1 .
    RefSeqi XP_001398868.1. XM_001398831.2.

    3D structure databases

    ProteinModelPortali A2RAR6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00013786.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00014047 ; CADANGAP00013786 ; CADANGAG00014047 .
    GeneIDi 4989974.
    KEGGi ang:ANI_1_534164.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    KOi K01210.
    OrthoDBi EOG7JT75H.

    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. "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 nameiEXGA_ASPNC
    AccessioniPrimary (citable) accession number: A2RAR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 45 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3