Reviewed, UniProtKB/Swiss-Prot P15329 (GUNX_CLOTM)

Names and origin

Protein names

Recommended name:
    Putative endoglucanase X
      Short name=EGX
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase
    Cellulase

Gene names

Name:

celX

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	224 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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 residues 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 lipid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cellulase activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro
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)
	P15329-1 [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: 3066698] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M22759 Genomic DNA. Translation: AAA23223.1.

PIR

A30476.

3D structure databases

PDBPDBe

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

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.2.1.4. 97464.

Family and domain databases

InterPro

IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR018247. EF_HAND_1.
IPR013831. Esterase_SGNH_hydro-type_subgr.
IPR001087. Lipase_GDSL.
[Graphical view]

Gene3D

G3DSA:1.10.1330.10. Cellulos_enz_dockerin_1. 1 hit.
G3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 1 hit.

Pfam

PF00404. Dockerin_1. 2 hits.
PF00657. Lipase_GDSL. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

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:	May 5, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)