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O08342

- GUNA_PAEBA

UniProt

O08342 - GUNA_PAEBA

Protein

Endoglucanase A

Gene

celA

Organism
Paenibacillus barcinonensis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Endoglucanase with high activity on carboxymethylcellulose (CMC) and lichenan, but not active on Avicel.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Strongly inhibited by Hg2+, Ag+ and Fe3+. To a lesser extent, is also inhibited by Pb2+, Mn2+, Sn2+ and Cu2+. By contrast, Ni2+, Zn2+, Co2+, Ba2+ and NH4+ do not affect enzyme activity, while 10 mM Ca2+, and Mg2+ produce a stimulating effect. Is also strongly inhibited by chemicals such as N-bromosuccinimide and dimethyl(2-dihydroxy-5-nitrobenzyl)sulphonium bromide. Is not affected by N-acetylimidazole.1 Publication

    pH dependencei

    Optimum pH is 4.0. Highly stable at acid pH. Retains 100% of its activity after 90 minutes incubation at pH 4.5 and 45 degrees Celsius, and 95% of the initial activity is found after 15 days incubation at room temperature and pH 4.5.1 Publication

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its maximum activity at 45 and 55 degrees Celsius, respectively.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei187 – 1871Proton donorBy similarity
    Active sitei328 – 3281NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    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:
    Endoglucanase A (EC:3.2.1.4)
    Alternative name(s):
    Cellulase A
    Endo-1,4-beta-D-glucanase A
    Gene namesi
    Name:celA
    OrganismiPaenibacillus barcinonensis
    Taxonomic identifieri198119 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Biotechnological usei

    Study of the performance of endoglucanase A on paper manufacture from agricultural fibers shows that treatment with the enzyme improves the properties of the pulp and the quality of paper. CelA treatment enhances the physical properties (stretch and tensile index) of paper from wheat straw, while dewatering properties are slightly diminished.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232CuratedAdd
    BLAST
    Chaini33 – 400368Endoglucanase APRO_0000371421Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO08342.
    SMRiO08342. Positions 40-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O08342-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKTFKKFSI AGLALLFMAT AAFAGWSTKA SAADMRSLTA AQITAEMGAG    50
    WNLGNQLEAT VNGTPNETSW GNPTITPELI KKVKAAGFKT IRIPVSYLNY 100
    IGSAPNYTVN ASWLNRIQQV VDYAYNEGLY VVINMHGDGF HSIPGSWLHV 150
    NSSNQNVIRD KYQKVWQQVA TRFSAYNERL IFESMNEVFD GNYNNPNTSY 200
    YGNLNAYNQI FVDTVRKTGG NNNARWLLVP GWNTNIDYTV GNYGFVVPTD 250
    NFRSSAIPSS QKRIMISAHY YSPWDFAGEE NGNITQWGAT ATNPAKRSTW 300
    GQEDYLDSQF KSMYDKFVTQ GYPVVMGEFG SIDKSSYDSS NNNYRAVYAK 350
    AVTATAKKYK LVPVYWDNGF NGQHGFALFN RFNNTVTQQN IINAIMQGMQ 400
    Length:400
    Mass (Da):44,799
    Last modified:July 1, 1997 - v1
    Checksum:iE89CB35BBC6F8AE5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12512 Genomic DNA. Translation: CAA73113.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12512 Genomic DNA. Translation: CAA73113.1 .

    3D structure databases

    ProteinModelPortali O08342.
    SMRi O08342. Positions 40-400.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterisation of the enzyme. Performance in paper manufacture from cereal straw."
      Blanco A., Diaz P., Martinez J., Vidal T., Torres A.L., Pastor F.I.J.
      Appl. Microbiol. Biotechnol. 50:48-54(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOTECHNOLOGY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
      Strain: DSM 15478 / CECT 7022 / BP-23.

    Entry informationi

    Entry nameiGUNA_PAEBA
    AccessioniPrimary (citable) accession number: O08342
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: July 1, 1997
    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 programProkaryotic Protein Annotation Program

    Miscellaneousi

    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