Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5B7R2

- CELB_EMENI

UniProt

Q5B7R2 - CELB_EMENI

Protein

Endo-beta-1,4-glucanase celB

Gene

celB

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 5.5.1 Publication

    Temperature dependencei

    Optimum temperature is 42 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei216 – 2161NucleophileBy similarity
    Active sitei221 – 2211Proton donorBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB

    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

    CAZyiGH7. Glycoside Hydrolase Family 7.
    mycoCLAPiEGL7A_EMENI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-beta-1,4-glucanase celB (EC:3.2.1.4)
    Short name:
    Endoglucanase celB
    Alternative name(s):
    Carboxymethylcellulase celB
    Cellulase B
    Gene namesi
    Name:celB
    Synonyms:eglB, eglC
    ORF Names:AN3418
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VI

    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 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 430414Endo-beta-1,4-glucanase celBPRO_0000395159Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00009621.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B7R2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG138370.
    HOGENOMiHOG000182210.
    OMAiPWINGEA.
    OrthoDBiEOG7Q8CXJ.

    Family and domain databases

    Gene3Di2.70.100.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view]
    PfamiPF00840. Glyco_hydro_7. 1 hit.
    [Graphical view]
    PRINTSiPR00734. GLHYDRLASE7.
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q5B7R2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLLSLSLL ATTISAQQIG TPEIRPRLTT YHCTSANGCT EQNTSVVLDA    50
    ATHPIHDASN PSVSCTTSNG LNPALCPDKQ TCADNCVIDG ITDYAAHGVE 100
    THGSRLTLTQ YRNVNGALSS VSPRVYLVDE SDPDEQEYRA LSLLAQEFTF 150
    TVNVSALPCG MNGALYLSEM SPSGGRSALN PAGASYGTGY CDAQCYVNPW 200
    INGEGNINGY GACCNEMDIW EANSRSTGFT PHACLYEPEE TEGRGVYECA 250
    SEDECDSAGE NDGICDKWGC GFNPYALGNT EYYGRGQGFE VDTKEPFTVV 300
    TQFLTDDGTS TGALTEIRRL YIQNGQVIEN AVVSSGADSL TDSLCASTAS 350
    WFDSYGGMEG MGRALGRGMV LAMSIWNDAG GYMQWLDGGD AGPCNATEGA 400
    PEFIEEHTPW TRVVFEDLKW GDIGSTFQAS 430
    Length:430
    Mass (Da):45,929
    Last modified:April 26, 2005 - v1
    Checksum:i4807FA907F18749E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451S → Y in AAM54071. (PubMed:12409103)Curated
    Sequence conflicti73 – 731P → R in AAM54071. (PubMed:12409103)Curated
    Sequence conflicti113 – 1131N → Y in AAM54071. (PubMed:12409103)Curated
    Sequence conflicti153 – 1531N → Y in AAM54071. (PubMed:12409103)Curated
    Sequence conflicti316 – 3161E → D in AAM54071. (PubMed:12409103)Curated
    Sequence conflicti345 – 3451C → W in AAM54071. (PubMed:12409103)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF420021 Genomic DNA. Translation: AAM54071.1.
    AACD01000055 Genomic DNA. Translation: EAA63386.1.
    BN001306 Genomic DNA. Translation: CBF82749.1.
    RefSeqiXP_661022.1. XM_655930.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00009621; CADANIAP00009621; CADANIAG00009621.
    GeneIDi2874128.
    KEGGiani:AN3418.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF420021 Genomic DNA. Translation: AAM54071.1 .
    AACD01000055 Genomic DNA. Translation: EAA63386.1 .
    BN001306 Genomic DNA. Translation: CBF82749.1 .
    RefSeqi XP_661022.1. XM_655930.1.

    3D structure databases

    ProteinModelPortali Q5B7R2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00009621.

    Protein family/group databases

    CAZyi GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi EGL7A_EMENI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00009621 ; CADANIAP00009621 ; CADANIAG00009621 .
    GeneIDi 2874128.
    KEGGi ani:AN3418.2.

    Phylogenomic databases

    eggNOGi NOG138370.
    HOGENOMi HOG000182210.
    OMAi PWINGEA.
    OrthoDBi EOG7Q8CXJ.

    Family and domain databases

    Gene3Di 2.70.100.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view ]
    Pfami PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00734. GLHYDRLASE7.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans."
      Lockington R.A., Rodbourn L., Barnett S., Carter C.J., Kelly J.M.
      Fungal Genet. Biol. 37:190-196(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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.
    4. "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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiCELB_EMENI
    AccessioniPrimary (citable) accession number: Q5B7R2
    Secondary accession number(s): C8VHK3, Q8NK01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 58 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