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A2QPC3

- EGLB_ASPNC

UniProt

A2QPC3 - EGLB_ASPNC

Protein

Probable endo-beta-1,4-glucanase B

Gene

eglB

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 36 (01 Oct 2014)
      Sequence version 1 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates By similarity.By similarity

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei160 – 1601Proton donorBy similarity
    Active sitei266 – 2661NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. hydrolase activity, acting on glycosyl bonds Source: ASPGD

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW
    2. glucan catabolic process Source: ASPGD
    3. xyloglucan catabolic process Source: ASPGD

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable endo-beta-1,4-glucanase B (EC:3.2.1.4)
    Short name:
    Endoglucanase B
    Alternative name(s):
    Carboxymethylcellulase B
    Cellulase B
    Gene namesi
    Name:eglB
    ORF Names:An07g08950
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 4L

    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 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 331313Probable endo-beta-1,4-glucanase BPRO_5000220219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliA2QPC3.
    SMRiA2QPC3. Positions 31-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000111120.
    KOiK01179.
    OrthoDBiEOG776T0S.

    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.

    A2QPC3-1 [UniParc]FASTAAdd to Basket

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    MKFQSTLLLA AAAGSALAVP HGSGHKKRAS VFEWFGSNES GAEFGTNIPG    50
    VWGTDYIFPD PSTISTLIGK GMNFFRVQFM MERLLPDSMT GSYDEEYLAN 100
    LTTVVKAVTD GGAHALIDPH NYGRYNGEII SSTSDFQTFW QNLAGQYKDN 150
    DLVMFDTNNE YYDMDQDLVL NLNQAAINGI RAAGASQYIF VEGNSWTGAW 200
    TWVDVNDNMK NLTDPEDKIV YEMHQYLDSD GSGTSETCVS GTIGKERITD 250
    ATQWLKDNKK VGFIGEYAGG SNDVCRSAVS GMLEYMANNT DVWKGASWWA 300
    AGPWWGDYIF SLEPPDGTAY TGMLDILETY L 331
    Length:331
    Mass (Da):36,559
    Last modified:September 23, 2008 - v1
    Checksum:iF3AE4BF70007C707
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270148 Genomic DNA. Translation: CAK45103.1.
    RefSeqiXP_001391969.1. XM_001391932.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00006168; CADANGAP00006047; CADANGAG00006168.
    GeneIDi4982163.
    KEGGiang:ANI_1_1120064.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270148 Genomic DNA. Translation: CAK45103.1 .
    RefSeqi XP_001391969.1. XM_001391932.2.

    3D structure databases

    ProteinModelPortali A2QPC3.
    SMRi A2QPC3. Positions 31-331.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00006168 ; CADANGAP00006047 ; CADANGAG00006168 .
    GeneIDi 4982163.
    KEGGi ang:ANI_1_1120064.

    Phylogenomic databases

    HOGENOMi HOG000111120.
    KOi K01179.
    OrthoDBi EOG776T0S.

    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 nameiEGLB_ASPNC
    AccessioniPrimary (citable) accession number: A2QPC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: September 23, 2008
    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3