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A2QX52

- EXGD_ASPNC

UniProt

A2QX52 - EXGD_ASPNC

Protein

Probable glucan 1,3-beta-glucosidase D

Gene

exgD

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 42 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei597 – 5971Proton donorBy similarity
    Active sitei702 – 7021NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

    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

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glucan 1,3-beta-glucosidase D (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase D
    Gene namesi
    Name:exgD
    ORF Names:An11g07660
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 7R

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 830830Probable glucan 1,3-beta-glucosidase DPRO_0000395165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi558 – 5581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi689 – 6891N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00008917.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QX52.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 307307CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini329 – 830502ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei308 – 32821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi38 – 8548Asp-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    KOiK01210.
    OrthoDBiEOG7ZPNTV.

    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.

    A2QX52-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGHSRSRDR LSPSSELDDA DPVYSPSVYQ REHYYNNDSL FDSADDDYTR    50
    TPRNVYSYET HDEYHDDDDD DDDVHEHDHD HEYDDKFEEP WVPLRAQVEG 100
    DQWREGFETA IPKEEDVTQA KEYQYQMSGA LGDDGPPPLP SDALGRGKGK 150
    KRLDRETRRQ RRKERLAAFF KHKNGSASAG LVSGDALAKL LGSQDGDEDC 200
    LSHLGTERAD SMSQKNLEGG RQRKLPVLSE EPMMLRPFPA VAPTGQTQGR 250
    VVSGAQLEEG GPGMEMRHRG GGGPPAEGLL QKEGDWDGST KGSSTSARPS 300
    FWKRYHKTFI FFAILIVLAA IAIPVGIIEA RRLHGTSGGD NSSNSNLKGI 350
    SRDSIPAYAR GTYLDPFTWY DTTDFNVTFT NATVGGLSIM GLNSTWNDSA 400
    QANENVPPLN EKFPYGSQPI RGVNLGGWLS IEPFIVPSLF DTYTSSEGII 450
    DEWTLSEKLG DSAASVIEKH YATFITEQDF ADIRDAGLDH VRIQFSYWAI 500
    KTYDGDPYVP KIAWRYLLRA IEYCRKYGLR VNLDPHGIPG SQNGWNHSGR 550
    QGTIGWLNGT DGELNRQRSL EMHDQLSQFF AQDRYKNVVT IYGLVNEPLM 600
    LSLPVEKVLN WTTEATNLVQ KNGIKAWVTV HDGFLNLDKW DKMLKTRPSN 650
    MMLDTHQYTV FNTGEIVLNH TRRVELICES WYSMIQQINI TSTGWGPTIC 700
    GEWSQADTDC AQYVNNVGRG TRWEGTFSLT DSTQYCPTAS EGTCSCTQAN 750
    AVPGVYSEGY KTFLQTYAEA QMSAFESAMG WFYWTWATES AAQWSYRTAW 800
    KNGYMPKKAY SPSFKCGDTI PSFGNLPEYY 830
    Length:830
    Mass (Da):93,303
    Last modified:March 6, 2007 - v1
    Checksum:iE07B09114631E566
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270244 Genomic DNA. Translation: CAK45960.1.
    RefSeqiXP_001394735.1. XM_001394698.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00009088; CADANGAP00008917; CADANGAG00009088.
    GeneIDi4984985.
    KEGGiang:ANI_1_2268094.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270244 Genomic DNA. Translation: CAK45960.1 .
    RefSeqi XP_001394735.1. XM_001394698.1.

    3D structure databases

    ProteinModelPortali A2QX52.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00008917.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00009088 ; CADANGAP00008917 ; CADANGAG00009088 .
    GeneIDi 4984985.
    KEGGi ang:ANI_1_2268094.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    KOi K01210.
    OrthoDBi EOG7ZPNTV.

    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 nameiEXGD_ASPNC
    AccessioniPrimary (citable) accession number: A2QX52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 42 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