P15329 (GUNX_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative endoglucanase X
Short name=EGX
EC=3.2.1.4

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

Gene names

Name:

celX

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	224 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.
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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
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 – 224	›224	Putative endoglucanase X		PRO_0000184076
Regions
	Repeat	168 – 191	24	1
	Repeat	202 – 224	23	2
	Region	168 – 224	57	2 X 24 AA approximate repeats
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P15329 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: F8822C5663FF2E80	FASTA	224	24,860
	10 20 30 40 50 60 IMKVTQDGSI PQIASNINNW LNTHNPDVVF LWIGGNDLLL SGNVNATGLS NLIDQIFTVK 70 80 90 100 110 120 PNVTLFVADY YPWPEAVKQY NAVIPGIVQQ KANAGKKVYF VKLSEIQFDR NTDISWDGLH 130 140 150 160 170 180 LSEIGYTKIA NIWYKYTIDI LKALAGQTQP TPSPSPTPTD SPLVKKGDVN LDGQVNSTDF 190 200 210 220 SLLKRYILKV VDINSINVTN ADMNNDGNIN STDISILKRI LLRN

References

[1]	"Conserved reiterated domains in Clostridium thermocellum endoglucanases are not essential for catalytic activity." Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J. Gene 69:29-38(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22759 Genomic DNA. Translation: AAA23223.1.

PIR

A30476.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VPT	X-ray	1.40	A	9-149	[»]

ProteinModelPortal

P15329.

SMR

P15329. Positions 9-146.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.1330.10. 1 hit.
3.40.50.1110. 1 hit.

InterPro

IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]

Pfam

PF00404. Dockerin_1. 2 hits.
[Graphical view]

SUPFAM

SSF63446. Cellulos_enz_dockerin_1. 1 hit.

PROSITE

PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit. Uncertain.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P15329.

Entry information

Entry name

GUNX_CLOTM

Accession

Primary (citable) accession number: P15329

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program