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A3DDN1 (GUND_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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 D

Short name=EGD
EC=3.2.1.4
Alternative name(s):
Cellulase D
Endo-1,4-beta-glucanase
Gene names
Name:celD
Ordered Locus Names:Cthe_0825
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length649 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 By similarity.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Cofactor

Calcium By similarity.

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 By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   LigandCalcium
   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 – 4141 By similarity
Chain42 – 649608Endoglucanase D
PRO_0000284722

Regions

Repeat585 – 608241
Repeat621 – 644242
Region585 – 644602 X 24 AA approximate repeats

Sites

Active site2011Nucleophile By similarity
Active site5161 By similarity
Active site5461 By similarity
Active site5551Proton donor By similarity

Experimental info

Sequence conflict5771A → P in CAA28255. Ref.1

Secondary structure

......... 649
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A3DDN1 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 3A6A44735B29D3F4

FASTA64972,415
        10         20         30         40         50         60 
MSRMTLKSSM KKRVLSLLIA VVFLSLTGVF PSGLIETKVS AAKITENYQF DSRIRLNSIG 

        70         80         90        100        110        120 
FIPNHSKKAT IAANCSTFYV VKEDGTIVYT GTATSMFDND TKETVYIADF SSVNEEGTYY 

       130        140        150        160        170        180 
LAVPGVGKSV NFKIAMNVYE DAFKTAMLGM YLLRCGTSVS ATYNGIHYSH GPCHTNDAYL 

       190        200        210        220        230        240 
DYINGQHTKK DSTKGWHDAG DYNKYVVNAG ITVGSMFLAW EHFKDQLEPV ALEIPEKNNS 

       250        260        270        280        290        300 
IPDFLDELKY EIDWILTMQY PDGSGRVAHK VSTRNFGGFI MPENEHDERF FVPWSSAATA 

       310        320        330        340        350        360 
DFVAMTAMAA RIFRPYDPQY AEKCINAAKV SYEFLKNNPA NVFANQSGFS TGEYATVSDA 

       370        380        390        400        410        420 
DDRLWAAAEM WETLGDEEYL RDFENRAAQF SKKIEADFDW DNVANLGMFT YLLSERPGKN 

       430        440        450        460        470        480 
PALVQSIKDS LLSTADSIVR TSQNHGYGRT LGTTYYWGCN GTVVRQTMIL QVANKISPNN 

       490        500        510        520        530        540 
DYVNAALDAI SHVFGRNYYN RSYVTGLGIN PPMNPHDRRS GADGIWEPWP GYLVGGGWPG 

       550        560        570        580        590        600 
PKDWVDIQDS YQTNEIAINW NAALIYALAG FVNYNSAQNE VLYGDVNDDG KVNSTDLTLL 

       610        620        630        640 
KRYVLKAVST LPSSKAEKNA DVNRDGRVNS SDVTILSRYL IRVIEKLPI 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the cellulase gene celD encoding endoglucanase D of Clostridium thermocellum."
Joliff G., Beguin P., Aubert J.-P.
Nucleic Acids Res. 14:8605-8613(1986) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04584 Genomic DNA. Translation: CAA28255.1.
CP000568 Genomic DNA. Translation: ABN52060.1.
PIRCZCLDM. A25535.
RefSeqYP_001037253.1. NC_009012.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FL4X-ray2.90A/D/G/J584-649[»]
ProteinModelPortalA3DDN1.
SMRA3DDN1. Positions 35-575, 580-649.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_0825.

Protein family/group databases

CAZyGH9. Glycoside Hydrolase Family 9.

Proteomic databases

PRIDEA3DDN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN52060; ABN52060; Cthe_0825.
GeneID4810443.
KEGGcth:Cthe_0825.
PATRIC19515357. VBICloThe47081_0867.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG05134.
HOGENOMHOG000245359.
KOK01179.
OMAQQDAKEC.
OrthoDBEOG6BCSN2.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-854-MONOMER.
MetaCyc:MONOMER-16416.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.40.10. 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.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceA3DDN1.

Entry information

Entry nameGUND_CLOTH
AccessionPrimary (citable) accession number: A3DDN1
Secondary accession number(s): P04954
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 49 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