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P15329

- GUNX_CLOTM

UniProt

P15329 - GUNX_CLOTM

Protein

Putative endoglucanase X

Gene

celX

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Catalytic activityi

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

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative endoglucanase X (EC:3.2.1.4)
    Short name:
    EGX
    Alternative name(s):
    Cellulase
    Endo-1,4-beta-glucanase
    Gene namesi
    Name:celX
    OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
    Taxonomic identifieri1515 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 224›224Putative endoglucanase XPRO_0000184076Add
    BLAST

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VPTX-ray1.40A9-149[»]
    ProteinModelPortaliP15329.
    SMRiP15329. Positions 9-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15329.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati168 – 191241Add
    BLAST
    Repeati202 – 224232Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni168 – 224572 X 24 AA approximate repeatsAdd
    BLAST

    Domaini

    A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    3.40.50.1110. 1 hit.
    InterProiIPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view]
    PfamiPF00404. Dockerin_1. 2 hits.
    [Graphical view]
    SUPFAMiSSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P15329-1 [UniParc]FASTAAdd to Basket

    « Hide

    IMKVTQDGSI PQIASNINNW LNTHNPDVVF LWIGGNDLLL SGNVNATGLS    50
    NLIDQIFTVK PNVTLFVADY YPWPEAVKQY NAVIPGIVQQ KANAGKKVYF 100
    VKLSEIQFDR NTDISWDGLH LSEIGYTKIA NIWYKYTIDI LKALAGQTQP 150
    TPSPSPTPTD SPLVKKGDVN LDGQVNSTDF SLLKRYILKV VDINSINVTN 200
    ADMNNDGNIN STDISILKRI LLRN 224
    Length:224
    Mass (Da):24,860
    Last modified:April 1, 1990 - v1
    Checksum:iF8822C5663FF2E80
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22759 Genomic DNA. Translation: AAA23223.1.
    PIRiA30476.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22759 Genomic DNA. Translation: AAA23223.1 .
    PIRi A30476.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VPT X-ray 1.40 A 9-149 [» ]
    ProteinModelPortali P15329.
    SMRi P15329. Positions 9-146.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P15329.

    Family and domain databases

    Gene3Di 1.10.1330.10. 1 hit.
    3.40.50.1110. 1 hit.
    InterProi IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view ]
    Pfami PF00404. Dockerin_1. 2 hits.
    [Graphical view ]
    SUPFAMi SSF63446. SSF63446. 1 hit.
    PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conserved reiterated domains in Clostridium thermocellum endoglucanases are not essential for catalytic activity."
      Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J.
      Gene 69:29-38(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGUNX_CLOTM
    AccessioniPrimary (citable) accession number: P15329
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 74 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

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3