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P15329 (GUNX_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length224 AA.
Sequence statusFragment.
Protein existenceEvidence 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 processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 224›224Putative endoglucanase X
PRO_0000184076

Regions

Repeat168 – 191241
Repeat202 – 224232
Region168 – 224572 X 24 AA approximate repeats

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P15329 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: F8822C5663FF2E80

FASTA22424,860
        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 

« Hide

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.
PIRA30476.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VPTX-ray1.40A9-149[»]
ProteinModelPortalP15329.
SMRP15329. Positions 9-146.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
3.40.50.1110. 1 hit.
InterProIPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamPF00404. Dockerin_1. 2 hits.
[Graphical view]
SUPFAMSSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15329.

Entry information

Entry nameGUNX_CLOTM
AccessionPrimary (citable) accession number: P15329
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 19, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries