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P50400

- GUND_CELFI

UniProt

P50400 - GUND_CELFI

Protein

Endoglucanase D

Gene

cenD

Organism
Cellulomonas fimi
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei208 – 2081Proton donorBy similarity
    Active sitei349 – 3491NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00696.

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase D (EC:3.2.1.4)
    Alternative name(s):
    Cellulase D
    Endo-1,4-beta-glucanase D
    Gene namesi
    Name:cenD
    OrganismiCellulomonas fimi
    Taxonomic identifieri1708 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3939Sequence AnalysisAdd
    BLAST
    Chaini40 – 747708Endoglucanase DPRO_0000007843Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP50400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini456 – 54388Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini552 – 63988Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini638 – 747110CBM2Add
    BLAST

    Sequence similaritiesi

    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR003961. Fibronectin_type3.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    PF00041. fn3. 2 hits.
    [Graphical view]
    SMARTiSM00637. CBD_II. 1 hit.
    SM00060. FN3. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51173. CBM2. 1 hit.
    PS50853. FN3. 2 hits.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P50400-1 [UniParc]FASTAAdd to Basket

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    MHSASRTRAR TRVRTAVSGL LAATVLAAPL TLVAAPAQAA TGDDWLHVEG    50
    NTIVDSTGKE AILSGVNWFG FNASERVFHG LWSGNITQIT QQMAQRGINV 100
    VRVPVSTQLL LEWKAGTFLK PNVNTYANPE LEGKNSLQIF EYWLTLCQKY 150
    GIKVFLDVHS AEADNSGHVY NMWWKGDITT EDVYEGWEWA ATRWKDDDTI 200
    VGADIKNEPH GTQGSTERAK WDGTTDKDNF KHFAETASKK ILAINPNWLV 250
    FVEGVEIYPK PGVPWTSTGL TDYYGTWWGG NLRGVRDHPI DLGAHQDQLV 300
    YSPHDYGPLV FDQKWFQKDF DKASLTADVW GPNWLFIHDE DIAPLLIGEW 350
    GGRLGQDPRQ DKWMAALRDL VAERRLSQTF WVLNPNSGDT GGLLLDDWKT 400
    WDEVKYSTML EPTLWKHGGK YVGLDHQVPL GGVGSTTGTS ISQVGGGTPD 450
    TTAPTAPTGL RAGTPTASTV PLTWSASTDT GGSGVAGYEV YRGTTLVGTT 500
    TATSYTVTGL AADSAYTFSV RAKDGAGNTS AASAAVTART AAGGGDVTAP 550
    SVPTGLTAGT PTATSVPLTW TASTDTGGSG VTGYEVYRGS TLVARPTGTS 600
    HTVTGLSAAT AYTFTVRAVD AAGNVSAASA PVGVTTAPDP TTGSCAVTYT 650
    ANGWSGGFTA AVTLTNTGTT ALSGWTLGFA FPSGQTLTQG WSARWAQSGS 700
    SVTATNEAWN AVLAPGASVE IGFSGTHTGT NTAPATFTVG GATCTTR 747
    Length:747
    Mass (Da):78,937
    Last modified:October 1, 1996 - v1
    Checksum:iBD15473C9D8B42BD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02544 Genomic DNA. Translation: AAA23089.1.
    PIRiB47093.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02544 Genomic DNA. Translation: AAA23089.1 .
    PIRi B47093.

    3D structure databases

    ProteinModelPortali P50400.
    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...

    Enzyme and pathway databases

    UniPathwayi UPA00696 .

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    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.
    IPR003961. Fibronectin_type3.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    PF00041. fn3. 2 hits.
    [Graphical view ]
    SMARTi SM00637. CBD_II. 1 hit.
    SM00060. FN3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS50853. FN3. 2 hits.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cellulose-binding polypeptides from Cellulomonas fimi: endoglucanase D (CenD), a family A beta-1,4-glucanase."
      Meinke A., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
      J. Bacteriol. 175:1910-1918(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGUND_CELFI
    AccessioniPrimary (citable) accession number: P50400
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 92 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3