P37699 (GUNC_CLOCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase C
EC=3.2.1.4

Alternative name(s):
Cellulase C
EGCCC
Endo-1,4-beta-glucanase C

Gene names

Name:	celCCC
Ordered Locus Names:	Ccel_0730

Organism

Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]

Taxonomic identifier

394503 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pathway	Glycan metabolism; cellulose degradation.
Subunit structure	Monomer.
Domain	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.
Post-translational modification	There are two forms of the cellulase. The shorter form lacks probably the C-terminal reiterated domains.
Sequence similarities	Belongs to the glycosyl hydrolase 8 (cellulase D) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing
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
	Signal peptide	1 – 32	32	Ref.3
	Chain	33 – 460	428	Endoglucanase C		PRO_0000007936
Regions
	Repeat	406 – 429	24	1
	Repeat	439 – 460	22	2
	Region	406 – 460	55	2 X 24 AA approximate repeats
Sites
	Active site	99	1	Proton donor By similarity
	Active site	155	1	Nucleophile Potential
Experimental info
	Sequence conflict	91	1	S → T in AAA73867. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P37699 [UniParc]. Last modified May 26, 2009. Version 2. Checksum: 2F31E1F6CB41504F	FASTA	460	50,483
	10 20 30 40 50 60 MIKGSSLKRF KSLVMAAIFS VSIISTAIAS SAADQIPFPY DAKYPNGAYS CLADSQSIGN 70 80 90 100 110 120 NLVRSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG LGYGLLLSVY FGEQQLFDDL 130 140 150 160 170 180 YRYVKVFLNS NGLMSWRIDS SGNIMGKDSI GAATDADEDI AVSLVFAHKK WGTSGGFNYQ 190 200 210 220 230 240 TEAKNYINNI YNKMVEPGTY VIKAGDTWGG SNVTNPSYFA PAWYRIFADF TGNSGWINVA 250 260 270 280 290 300 NKCYEIADKA RNSNTGLVPD WCTANGTPAS GQGFDFYYDA IRYQWRAAID YSWYGTAKAK 310 320 330 340 350 360 THCDAISNFF KNIGYANIKD GYTISGSQIS SNHTATFVSC AAAAAMTGTD TTYAKNIYNE 370 380 390 400 410 420 CVKVKDSGNY TYFGNTLRMM VLLYTTGNFP NLYTYNSQPK PDLKGDVNND GAIDALDIAA 430 440 450 460 LKKAILTQTT SNISLTNADM NNDGNIDAID FAQLKVKLLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum." Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T., Belaich J.-P. Gene 119:17-28(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
[2]	"Complete sequence of Clostridium cellulolyticum H10." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. , Ivanova N., Zhou J., Richardson P. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
[3]	"Purification and characterization of endoglucanase C from Clostridium cellulolyticum. Catalytic comparison with endoglucanase A." Fierobe H.-P., Bagnara-Tardif C., Gaudin C., Guerlesquin F., Sauve P., Belaich A., Belaich J.-P. Eur. J. Biochem. 217:557-565(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-37, CHARACTERIZATION. Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M87018 Genomic DNA. Translation: AAA73867.1. CP001348 Genomic DNA. Translation: ACL75109.1.
PIR	JC1299.
RefSeq	YP_002505089.1. NC_011898.1.
3D structure databases
ProteinModelPortal	P37699.
SMR	P37699. Positions 39-391.
ModBase	Search...
Protein-protein interaction databases
STRING	394503.Ccel_0730.
Protein family/group databases
CAZy	GH8. Glycoside Hydrolase Family 8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACL75109; ACL75109; Ccel_0730.
GeneID	7309584.
KEGG	cce:Ccel_0730.
PATRIC	19432257. VBICloCel57783_0755.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3405.
HOGENOM	HOG000069581.
OMA	GNFPNLY.
ProtClustDB	CLSK852404.
Enzyme and pathway databases
BioCyc	CCEL394503:GJET-751-MONOMER.
UniPathway	UPA00696.
Family and domain databases
Gene3D	1.10.1330.10. 1 hit. 1.50.10.10. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR016134. Cellulos_enz_dockerin_1. IPR002105. Cellulos_enz_dockerin_1_Ca-bd. IPR018242. Dockerin_1. IPR018247. EF_Hand_1_Ca_BS. IPR002037. Glyco_hydro_8. IPR019834. Glyco_hydro_8_CS. [Graphical view]
Pfam	PF00404. Dockerin_1. 2 hits. PF01270. Glyco_hydro_8. 1 hit. [Graphical view]
PRINTS	PR00735. GLHYDRLASE8.
SUPFAM	SSF63446. Cellulos_enz_dockerin_1. 1 hit. SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS00448. CLOS_CELLULOSOME_RPT. 1 hit. PS00018. EF_HAND_1. 2 hits. Uncertain. PS00812. GLYCOSYL_HYDROL_F8. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNC_CLOCE

Accession

Primary (citable) accession number: P37699
Secondary accession number(s): B8I7V2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program