P0C2S2 (GUNA_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase A
Short name=EGA
EC=3.2.1.4

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

Gene names

Name:

celA

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	14 AA.
Sequence status	Fragment.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 8 (cellulase D) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – ›14	›14	Endoglucanase A		PRO_0000007935
Experimental info
	Non-terminal residue	14	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2S2 [UniParc]. Last modified April 17, 2007. Version 1. Checksum: 9917F3399EBAA621	FASTA	14	1,450
	10 AGVPFNTKTP YGPT

References

[1]	"Dissociation of the cellulosome of Clostridium thermocellum in the presence of ethylenediaminetetraacetic acid occurs with the formation of trucated polypeptides." Choi S.K., Ljungdahl L.G. Biochemistry 35:4897-4905(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: JW20.

Cross-references

3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P0C2S2. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00448. CLOS_CELLULOSOME_RPT. Partial match. PS00018. EF_HAND_1. Partial match. PS00812. GLYCOSYL_HYDROL_F8. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNA_CLOTM

Accession

Primary (citable) accession number: P0C2S2
Secondary accession number(s): P04955

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	April 17, 2007
Last modified:	April 3, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program