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Protein

Endoglucanase C

Gene

celC

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: 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: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei140Proton donor1
Active sitei280Nucleophile1 Publication1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001840471 – 343Endoglucanase CAdd BLAST343

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_2807.

Structurei

Secondary structure

1343
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Beta strandi13 – 16Combined sources4
Helixi22 – 28Combined sources7
Helixi31 – 40Combined sources10
Beta strandi44 – 50Combined sources7
Helixi51 – 53Combined sources3
Beta strandi57 – 59Combined sources3
Helixi65 – 80Combined sources16
Beta strandi84 – 91Combined sources8
Turni105 – 107Combined sources3
Helixi109 – 125Combined sources17
Turni126 – 128Combined sources3
Beta strandi131 – 136Combined sources6
Beta strandi144 – 146Combined sources3
Helixi147 – 163Combined sources17
Beta strandi169 – 172Combined sources4
Helixi174 – 177Combined sources4
Helixi179 – 184Combined sources6
Beta strandi191 – 199Combined sources9
Helixi203 – 206Combined sources4
Turni207 – 209Combined sources3
Helixi214 – 219Combined sources6
Beta strandi225 – 228Combined sources4
Helixi232 – 238Combined sources7
Helixi240 – 248Combined sources9
Beta strandi252 – 254Combined sources3
Helixi255 – 272Combined sources18
Beta strandi275 – 281Combined sources7
Helixi289 – 305Combined sources17
Beta strandi309 – 313Combined sources5
Beta strandi315 – 317Combined sources3
Helixi332 – 339Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CECX-ray2.15A1-343[»]
1CENX-ray2.30A1-343[»]
1CEOX-ray1.90A1-343[»]
ProteinModelPortaliP0C2S3.
SMRiP0C2S3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2S3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CTM. Bacteria.
COG2730. LUCA.

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:
EMBLi
GenBanki
DDBJi
Links Updated
M19422 Genomic DNA. Translation: AAA23220.1.
PIRiJT0268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19422 Genomic DNA. Translation: AAA23220.1.
PIRiJT0268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CECX-ray2.15A1-343[»]
1CENX-ray2.30A1-343[»]
1CEOX-ray1.90A1-343[»]
ProteinModelPortaliP0C2S3.
SMRiP0C2S3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203119.Cthe_2807.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CTM. Bacteria.
COG2730. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00696.

Miscellaneous databases

EvolutionaryTraceiP0C2S3.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 49 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.