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Q5BCX8

- EGLD_EMENI

UniProt

Q5BCX8 - EGLD_EMENI

Protein

Endo-beta-1,4-glucanase D

Gene

eglD

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      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.1 Publication

    Catalytic activityi

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

    pH dependencei

    Optimum pH is under 6.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei163 – 1631Proton donorBy similarity
    Active sitei209 – 2091NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    mycoCLAPiPMO9A_EMENI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    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:AN1602
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VII

    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 – 357339Endo-beta-1,4-glucanase DPRO_0000394067Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi327 ↔ 344By similarity
    Disulfide bondi338 ↔ 354By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ5BCX8.
    SMRiQ5BCX8. Positions 322-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini319 – 35537CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 234216CatalyticAdd
    BLAST
    Regioni235 – 31884Ser/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.

    Q5BCX8-1 [UniParc]FASTAAdd to Basket

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    MKFSSVLALA ASAKLVASHA TVFAVWINDE DQGLGNTADG YIRTPPNNSP    50
    VTDVTSTDLT CNVNGDQAAA KTLEVAAGDK ITFEWHHNSR DSSDDIIADS 100
    HKGPVLVYMA PTEAGSAGKN WVKIYEDGYN DGTWAVDTLI ANKGKHSVTV 150
    PDVPAGNYLF RPEIIALHEG NREGGAQLYM ECVQFKVTSD GTTQLPEGVS 200
    LPGAYTATDE GILFDIYSSF DSYPIPGPAV WDGASSGSGS SGSGSSSSAA 250
    ATSSAEKTAT STTAAATTTA VATSTSSATQ VQPTSVATFT TSVRPTTSAA 300
    PTTSAPTSSA APTGGTGTGS IQIYQQCGGM NYKGATGCAS GLTCKQWNPY 350
    YHQCVQA 357
    Length:357
    Mass (Da):36,732
    Last modified:April 26, 2005 - v1
    Checksum:i64BAB1984CDB49BD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490474 mRNA. Translation: ABF50850.1.
    AACD01000026 Genomic DNA. Translation: EAA64722.1.
    BN001307 Genomic DNA. Translation: CBF85202.1.
    RefSeqiXP_659206.1. XM_654114.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00008239; CADANIAP00008239; CADANIAG00008239.
    GeneIDi2875535.
    KEGGiani:AN1602.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490474 mRNA. Translation: ABF50850.1 .
    AACD01000026 Genomic DNA. Translation: EAA64722.1 .
    BN001307 Genomic DNA. Translation: CBF85202.1 .
    RefSeqi XP_659206.1. XM_654114.1.

    3D structure databases

    ProteinModelPortali Q5BCX8.
    SMRi Q5BCX8. Positions 322-355.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    mycoCLAPi PMO9A_EMENI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00008239 ; CADANIAP00008239 ; CADANIAG00008239 .
    GeneIDi 2875535.
    KEGGi ani:AN1602.2.

    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. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
      Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiEGLD_EMENI
    AccessioniPrimary (citable) accession number: Q5BCX8
    Secondary accession number(s): C8VN99, Q1HFV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 64 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