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Q2US83

- EGLD_ASPOR

UniProt

Q2US83 - EGLD_ASPOR

Protein

Probable endo-beta-1,4-glucanase D

Gene

eglD

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      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 sitei164 – 1641Proton donorBy similarity
    Active sitei210 – 2101NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable endo-beta-1,4-glucanase D (EC:3.2.1.4)
    Short name:
    Endoglucanase D
    Alternative name(s):
    Carboxymethylcellulase D
    Cellulase D
    Gene namesi
    Name:eglD
    ORF Names:AO090005000531
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 1

    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 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 367347Probable endo-beta-1,4-glucanase DPRO_0000394065Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi337 ↔ 354By similarity
    Disulfide bondi348 ↔ 364By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ2US83.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini329 – 36537CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 235215CatalyticAdd
    BLAST
    Regioni236 – 32590Ser/Thr-rich linkerAdd
    BLAST

    Domaini

    Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 61 family.Curated
    Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG120437.
    HOGENOMiHOG000158937.
    OMAiGYIDSPP.
    OrthoDBiEOG7KM64H.

    Family and domain databases

    InterProiIPR000254. Cellulose-bd_dom_fun.
    IPR005103. Glyco_hydro_61.
    [Graphical view]
    PfamiPF00734. CBM_1. 1 hit.
    PF03443. Glyco_hydro_61. 1 hit.
    [Graphical view]
    SMARTiSM00236. fCBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57180. SSF57180. 1 hit.
    PROSITEiPS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q2US83-1 [UniParc]FASTAAdd to Basket

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    MKSSTFGMLA LAAAAKLVSA HATVHAVWIN DVDQGEGNSE SGYIRSPPSN    50
    SPITDVTSKD MTCNVNNKAT AKTLEVKAGD KITFEWHHDS RSDSDDIIAS 100
    SHKGPIMVYM APTEKGTAGN GWVKIAEDGY TDGTWAVDTL IKNRGKHSVT 150
    VPDVAAGEYL FRPEIIALHE GNRQGGAQFY MECVQVKVTS SGSKTLPEGV 200
    SIPGAYTATD KGILFDIYNS FDSYPFPGPA VWDGASGSSS SPSASASASA 250
    PAATSAAPAP SSFTTIAKQP ATSSTEAPST ENTSTTSTIV STTAAASATA 300
    PATPSSTSAI ASSAASTNSV PQPSSNAGGA VKEWYQCGGL NYKGSTQCEE 350
    GLTCKKWNPY YYQCISA 367
    Length:367
    Mass (Da):38,033
    Last modified:January 24, 2006 - v1
    Checksum:i0C038474B7C681F3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007151 Genomic DNA. Translation: BAE55582.1.

    Genome annotation databases

    EnsemblFungiiCADAORAT00002518; CADAORAP00002480; CADAORAG00002518.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007151 Genomic DNA. Translation: BAE55582.1 .

    3D structure databases

    ProteinModelPortali Q2US83.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00002518 ; CADAORAP00002480 ; CADAORAG00002518 .

    Phylogenomic databases

    eggNOGi NOG120437.
    HOGENOMi HOG000158937.
    OMAi GYIDSPP.
    OrthoDBi EOG7KM64H.

    Family and domain databases

    InterProi IPR000254. Cellulose-bd_dom_fun.
    IPR005103. Glyco_hydro_61.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF03443. Glyco_hydro_61. 1 hit.
    [Graphical view ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    Entry informationi

    Entry nameiEGLD_ASPOR
    AccessioniPrimary (citable) accession number: Q2US83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 40 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