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P0C2S3

- GUNC_CLOTM

UniProt

P0C2S3 - GUNC_CLOTM

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Protein

Endoglucanase C

Gene

celC

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

        10         20         30         40         50
MVSFKAGINL GGWISQYQVF SKEHFDTFIT EKDIETIAEA GFDHVRLPFD
60 70 80 90 100
YPIIESDDNV GEYKEDGLSY IDRCLEWCKK YNLGLVLDMH HAPGYRFQDF
110 120 130 140 150
KTSTLFEDPN QQKRFVDIWR FLAKRYINER EHIAFELLNE VVEPDSTRWN
160 170 180 190 200
KLMLEYIKAI REIDSTMWLY IGGNNYNSPD ELKNLADIDD DYIVYNFHFY
210 220 230 240 250
NPFFFTHQKA HWSESAMAYN RTVKYPGQYE GIEEFVKNNP KYSFMMELNN
260 270 280 290 300
LKLNKELLRK DLKPAIEFRE KKKCKLYCGE FGVIAIADLE SRIKWHEDYI
310 320 330 340
SLLEEYDIGG AVWNYKKMDF EIYNEDRKPV SQELVNILAR RKT
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