P0C2S3 (GUNC_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase C
EC=3.2.1.4

Alternative name(s):
Cellulase C
Endo-1,4-beta-glucanase C
Short name=EgC

Gene names

Name:

celC

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pathway	Glycan metabolism; cellulose degradation.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 343

343

Endoglucanase C

PRO_0000184047

Sites

Active site

140

1

Proton donor

Active site

280

1

Nucleophile Ref.2

Secondary structure

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343

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Beta strand

13 – 16

4

Helix

22 – 28

7

Helix

31 – 40

10

Beta strand

44 – 50

7

Helix

51 – 53

3

Beta strand

57 – 59

3

Helix

65 – 80

16

Beta strand

84 – 91

8

Turn

105 – 107

3

Helix

109 – 125

17

Turn

126 – 128

3

Beta strand

131 – 136

6

Beta strand

144 – 146

3

Helix

147 – 163

17

Beta strand

169 – 172

4

Helix

174 – 177

4

Helix

179 – 184

6

Beta strand

191 – 199

9

Helix

203 – 206

4

Turn

207 – 209

3

Helix

214 – 219

6

Beta strand

225 – 228

4

Helix

232 – 238

7

Helix

240 – 248

9

Beta strand

252 – 254

3

Helix

255 – 272

18

Beta strand

275 – 281

7

Helix

289 – 305

17

Beta strand

309 – 313

5

Beta strand

315 – 317

3

Helix

332 – 339

8

Sequences

	Sequence		Length	Mass (Da)
	P0C2S3 [UniParc]. Last modified April 17, 2007. Version 1. Checksum: BD24763F548C726E	FASTA	343	40,954
	10 20 30 40 50 60 MVSFKAGINL GGWISQYQVF SKEHFDTFIT EKDIETIAEA GFDHVRLPFD YPIIESDDNV 70 80 90 100 110 120 GEYKEDGLSY IDRCLEWCKK YNLGLVLDMH HAPGYRFQDF KTSTLFEDPN QQKRFVDIWR 130 140 150 160 170 180 FLAKRYINER EHIAFELLNE VVEPDSTRWN KLMLEYIKAI REIDSTMWLY IGGNNYNSPD 190 200 210 220 230 240 ELKNLADIDD DYIVYNFHFY NPFFFTHQKA HWSESAMAYN RTVKYPGQYE GIEEFVKNNP 250 260 270 280 290 300 KYSFMMELNN LKLNKELLRK DLKPAIEFRE KKKCKLYCGE FGVIAIADLE SRIKWHEDYI 310 320 330 340 SLLEEYDIGG AVWNYKKMDF EIYNEDRKPV SQELVNILAR RKT

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19422 Genomic DNA. Translation: AAA23220.1.

PIR

JT0268.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0C2S3.

SMR

P0C2S3. Positions 1-340.

ModBase

Search...

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00696.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00150. Cellulase. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0C2S3.

Entry information

Entry name

GUNC_CLOTM

Accession

Primary (citable) accession number: P0C2S3
Secondary accession number(s): P07985

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	April 17, 2007
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program