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A3DC29 (GUNA_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Endoglucanase A

Short name=EGA
EC=3.2.1.4
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase
Gene names
Name:celA
Ordered Locus Names:Cthe_0269
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Sequence similarities

Belongs to the glycosyl hydrolase 8 (cellulase D) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
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

Signal peptide1 – 3232 By similarity
Chain33 – 477445Endoglucanase A
PRO_0000284721

Regions

Repeat417 – 440241
Repeat449 – 472242
Region417 – 472562 X 24 AA approximate repeats

Sites

Active site951Proton donor
Active site1521Nucleophile Probable

Secondary structure

........................................................ 477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A3DC29 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: BA5A0AD5022E8A51

FASTA47752,594
        10         20         30         40         50         60 
MKNVKKRVGV VLLILAVLGV YMLAMPANTV SAAGVPFNTK YPYGPTSIAD NQSEVTAMLK 

        70         80         90        100        110        120 
AEWEDWKSKR ITSNGAGGYK RVQRDASTNY DTVSEGMGYG LLLAVCFNEQ ALFDDLYRYV 

       130        140        150        160        170        180 
KSHFNGNGLM HWHIDANNNV TSHDGGDGAA TDADEDIALA LIFADKLWGS SGAINYGQEA 

       190        200        210        220        230        240 
RTLINNLYNH CVEHGSYVLK PGDRWGGSSV TNPSYFAPAW YKVYAQYTGD TRWNQVADKC 

       250        260        270        280        290        300 
YQIVEEVKKY NNGTGLVPDW CTASGTPASG QSYDYKYDAT RYGWRTAVDY SWFGDQRAKA 

       310        320        330        340        350        360 
NCDMLTKFFA RDGAKGIVDG YTIQGSKISN NHNASFIGPV AAASMTGYDL NFAKELYRET 

       370        380        390        400        410        420 
VAVKDSEYYG YYGNSLRLLT LLYITGNFPN PLSDLSGQPT PPSNPTPSLP PQVVYGDVNG 

       430        440        450        460        470 
DGNVNSTDLT MLKRYLLKSV TNINREAADV NRDGAINSSD MTILKRYLIK SIPHLPY 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of a cellulase gene of the thermophilic bacterium Clostridium thermocellum."
Beguin P., Cornet P., Aubert J.-P.
J. Bacteriol. 162:102-105(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Clostridium thermocellum ATCC 27405."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.
[3]"The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum."
Alzari P.M., Souchon H., Dominguez R.
Structure 4:265-275(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 33-395.
[4]"Advantages of high-resolution phasing: MAD to atomic resolution."
Schmidt A., Gonzalez A., Morris R.J., Costabel M., Alzari P.M., Lamzin V.S.
Acta Crystallogr. D 58:1433-1441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF 33-395.
[5]"Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate."
Guerin D.M., Lascombe M.B., Costabel M., Souchon H., Lamzin V., Beguin P., Alzari P.M.
J. Mol. Biol. 316:1061-1069(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS) OF 33-395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03088 Genomic DNA. Translation: AAA83521.1.
CP000568 Genomic DNA. Translation: ABN51508.1.
PIRCZCLAM. A23100.
RefSeqYP_001036701.1. NC_009012.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CEMX-ray1.65A33-395[»]
1IS9X-ray1.03A33-395[»]
1KWFX-ray0.94A33-395[»]
ProteinModelPortalA3DC29.
SMRA3DC29. Positions 33-395, 412-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_0269.

Protein family/group databases

CAZyGH8. Glycoside Hydrolase Family 8.

Proteomic databases

PRIDEA3DC29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN51508; ABN51508; Cthe_0269.
GeneID4808552.
KEGGcth:Cthe_0269.
PATRIC19514173. VBICloThe47081_0284.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3405.
HOGENOMHOG000069581.
OMADMDIAYA.
OrthoDBEOG67Q9BX.
ProtClustDBCLSK852404.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-276-MONOMER.
MetaCyc:MONOMER-16413.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
InterProIPR008928. 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]
PfamPF00404. Dockerin_1. 2 hits.
PF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSPR00735. GLHYDRLASE8.
SUPFAMSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceA3DC29.

Entry information

Entry nameGUNA_CLOTH
AccessionPrimary (citable) accession number: A3DC29
Secondary accession number(s): P04955
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 20, 2007
Last modified: February 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries