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P0C2S3

- GUNC_CLOTM

UniProt

P0C2S3 - GUNC_CLOTM

Protein

Endoglucanase C

Gene

celC

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 42 (01 Oct 2014)
      Sequence version 1 (17 Apr 2007)
      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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei140 – 1401Proton donor
    Active sitei280 – 2801Nucleophile1 Publication

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    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

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase C (EC:3.2.1.4)
    Alternative name(s):
    Cellulase C
    Endo-1,4-beta-glucanase C
    Short name:
    EgC
    Gene namesi
    Name:celC
    OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
    Taxonomic identifieri1515 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 343343Endoglucanase CPRO_0000184047Add
    BLAST

    Structurei

    Secondary structure

    1
    343
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Beta strandi13 – 164
    Helixi22 – 287
    Helixi31 – 4010
    Beta strandi44 – 507
    Helixi51 – 533
    Beta strandi57 – 593
    Helixi65 – 8016
    Beta strandi84 – 918
    Turni105 – 1073
    Helixi109 – 12517
    Turni126 – 1283
    Beta strandi131 – 1366
    Beta strandi144 – 1463
    Helixi147 – 16317
    Beta strandi169 – 1724
    Helixi174 – 1774
    Helixi179 – 1846
    Beta strandi191 – 1999
    Helixi203 – 2064
    Turni207 – 2093
    Helixi214 – 2196
    Beta strandi225 – 2284
    Helixi232 – 2387
    Helixi240 – 2489
    Beta strandi252 – 2543
    Helixi255 – 27218
    Beta strandi275 – 2817
    Helixi289 – 30517
    Beta strandi309 – 3135
    Beta strandi315 – 3173
    Helixi332 – 3398

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CECX-ray2.15A1-343[»]
    1CENX-ray2.30A1-343[»]
    1CEOX-ray1.90A1-343[»]
    ProteinModelPortaliP0C2S3.
    SMRiP0C2S3. Positions 1-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C2S3.

    Family & Domainsi

    Sequence similaritiesi

    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. 2 hits.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0C2S3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSFKAGINL GGWISQYQVF SKEHFDTFIT EKDIETIAEA GFDHVRLPFD    50
    YPIIESDDNV GEYKEDGLSY IDRCLEWCKK YNLGLVLDMH HAPGYRFQDF 100
    KTSTLFEDPN QQKRFVDIWR FLAKRYINER EHIAFELLNE VVEPDSTRWN 150
    KLMLEYIKAI REIDSTMWLY IGGNNYNSPD ELKNLADIDD DYIVYNFHFY 200
    NPFFFTHQKA HWSESAMAYN RTVKYPGQYE GIEEFVKNNP KYSFMMELNN 250
    LKLNKELLRK DLKPAIEFRE KKKCKLYCGE FGVIAIADLE SRIKWHEDYI 300
    SLLEEYDIGG AVWNYKKMDF EIYNEDRKPV SQELVNILAR RKT 343
    Length:343
    Mass (Da):40,954
    Last modified:April 17, 2007 - v1
    Checksum:iBD24763F548C726E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19422 Genomic DNA. Translation: AAA23220.1.
    PIRiJT0268.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19422 Genomic DNA. Translation: AAA23220.1 .
    PIRi JT0268.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CEC X-ray 2.15 A 1-343 [» ]
    1CEN X-ray 2.30 A 1-343 [» ]
    1CEO X-ray 1.90 A 1-343 [» ]
    ProteinModelPortali P0C2S3.
    SMRi P0C2S3. Positions 1-340.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00696 .

    Miscellaneous databases

    EvolutionaryTracei P0C2S3.

    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. 2 hits.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the celC gene encoding endoglucanase C of Clostridium thermocellum."
      Schwarz W.H., Schimming S., Ruecknagel K.P., Burgschwaiger S., Kreil G., Staudenbauer W.L.
      Gene 63:23-30(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Glu280 is the nucleophile in the active site of Clostridium thermocellum CelC, a family A endo-beta-1,4-glucanase."
      Wang Q., Tull D., Meinke A., Gilkes N.R., Warren R.A., Aebersold R., Withers S.G.
      J. Biol. Chem. 268:14096-14102(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE GLU-280.
    3. "A common protein fold and similar active site in two distinct families of beta-glycanases."
      Dominguez R., Souchon H., Spinelli S., Dauter Z., Wilson K.S., Chauvaux S., Beguin P., Alzari P.M.
      Nat. Struct. Biol. 2:569-576(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
    4. "The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism."
      Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M.
      J. Mol. Biol. 257:1042-1051(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLN-140.

    Entry informationi

    Entry nameiGUNC_CLOTM
    AccessioniPrimary (citable) accession number: P0C2S3
    Secondary accession number(s): P07985
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    CelC has an unusual substrate range and displays features common to cellobiohydrolases by being able to cleave the agluconic bond of aryl-beta-glucosides.

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3