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P54937

- GUNA_CLOLO

UniProt

P54937 - GUNA_CLOLO

Protein

Endoglucanase A

Gene

celA

Organism
Clostridium longisporum
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Hydrolyzes barley beta-glucan, lichenan, carboxymethylcellulose and xylan. It shows preferential activity against the larger cellooligosaccharides (cellohexaose and cellopentaose); cellotetraose is the smallest substrate degraded completely.

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 4.8.

    Temperature dependencei

    Optimum temperature is 43 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei185 – 1851Proton donorBy similarity
    Active sitei309 – 3091NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. polysaccharide 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

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    GH5. 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-glucanase A
    Gene namesi
    Name:celA
    OrganismiClostridium longisporum
    Taxonomic identifieri1523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 517492Endoglucanase APRO_0000007849Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP54937.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini416 – 517102CBM2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – ?CatalyticBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SMARTiSM00637. CBD_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51173. CBM2. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P54937-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRSLLKTCS IIAGATIIFS SLSISRNPLE VQAASMRSAS EIVQEMGVGW    50
    NLGNTLDAKI TNLSYNTSPI SFETGWGNPV TTKAMIDKIK NAGFKTIRIP 100
    TTWGEHLDGN NKLNEEWVKR VKEVVDYCIA DDLYVILNTH HEGNWVIPTY 150
    AKESSVTPKL KTLWTQISEA FKDYDDHLIF ETLNEPRLEG TPYEWTGGTS 200
    ESRDVVNKYN AAALESIRKT GGNNLSRAVM MPTYAASGSS TTMNDFKVPD 250
    DKNVIASVHA YSPYFFAMDT SSNSVNTWGS SYDKYSLDVE LDSYLNTFKS 300
    KGVPVVIGEF GSINKNNTSS RAELAEYYVT AAQKRGIPCV WWDNNYAETN 350
    KGETFGLLNR STLNWYFSDI KDALIRGYKN VHPEATEDDK PSTDVTNPDS 400
    GNTKPDSGNT NPGTETTTPT DNEKISITSK INDWGGAYQA DFTLKNNTSS 450
    DINNWSFKIK KNDIVFTNYW DVKITEENGY YVVTPQAWKT TILANSSIVI 500
    SIQGTGKVIS NFEYKFD 517
    Length:517
    Mass (Da):57,660
    Last modified:October 1, 1996 - v1
    Checksum:iA1D1570302FFBA30
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02868 Unassigned DNA. Translation: AAC37035.1.
    PIRiI40798.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02868 Unassigned DNA. Translation: AAC37035.1 .
    PIRi I40798.

    3D structure databases

    ProteinModelPortali P54937.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SMARTi SM00637. CBD_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of an endo-(1-->4)-beta-glucanase gene, celA, from the rumen bacterium Clostridium sp. ('C. longisporum') and characterization of its product, CelA, in Escherichia coli."
      Mittendorf V., Thomson J.A.
      J. Gen. Microbiol. 139:3233-3242(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 49440 / B6405.

    Entry informationi

    Entry nameiGUNA_CLOLO
    AccessioniPrimary (citable) accession number: P54937
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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