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P0C2S4 (GUND_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length625 AA.
Sequence statusFragment.
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.

Cofactor

Calcium.

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 9 (cellulase E) family.

Caution

The sequence shown here has been extracted from PDB entry 1CLC.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   LigandCalcium
   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

Signal peptide‹1 – 17›17
Chain18 – 625608Endoglucanase D
PRO_0000007949

Regions

Repeat561 – 584241
Repeat597 – 620242
Region561 – 620602 X 24 AA approximate repeats

Sites

Active site1771Nucleophile
Active site4921 Ref.2
Active site5221 Ref.4
Active site5311Proton donor Ref.3

Experimental info

Mutagenesis411H → A: 79% of wild-type activity. Ref.2 Ref.3
Mutagenesis1431H → A: 104% of wild-type activity. Ref.2 Ref.3
Mutagenesis1461H → A: 77% of wild-type activity. Ref.2 Ref.3
Mutagenesis1501H → A: 2% of wild-type activity. Ref.2 Ref.3
Mutagenesis1631H → A: 124% of wild-type activity. Ref.2 Ref.3
Mutagenesis1731H → A: 8% of wild-type activity. Ref.2 Ref.3
Mutagenesis1741D → A: 0.08% of wild-type activity. Ref.2 Ref.3
Mutagenesis1771D → A: 0.2% of wild-type activity. Ref.2 Ref.3
Mutagenesis1981H → S: 17% of wild-type activity. Ref.2 Ref.3
Mutagenesis2221D → A: 72% of wild-type activity. Ref.2 Ref.3
Mutagenesis2451H → A: 90% of wild-type activity. Ref.2 Ref.3
Mutagenesis2621H → A: 19% of wild-type activity. Ref.2 Ref.3
Mutagenesis2931D → A: 98% of wild-type activity. Ref.2 Ref.3
Mutagenesis3371D → A: 86% of wild-type activity. Ref.2 Ref.3
Mutagenesis4211H → S: 32% of wild-type activity. Ref.2 Ref.3
Mutagenesis4681H → A: 9% of wild-type activity. Ref.2 Ref.3
Mutagenesis4921H → S: 25% of wild-type activity. Ref.2 Ref.3
Mutagenesis4931D → A: 0.8% of wild-type activity. Ref.2 Ref.3
Mutagenesis4991D → A: 224% of wild-type activity. Ref.2 Ref.3
Mutagenesis5031E → A: 127% of wild-type activity. Ref.2 Ref.3
Mutagenesis5191D → A: 91% of wild-type activity. Ref.2 Ref.3
Mutagenesis5221D → A: 1% of wild-type activity. Ref.2 Ref.3
Mutagenesis5251D → A: 118% of wild-type activity. Ref.2 Ref.3
Mutagenesis5311E → A: 0.3% of wild-type activity. Ref.2 Ref.3
Non-terminal residue11

Secondary structure

............................................................................ 625
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C2S4 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 6BFD88E2BDF1BD8F

FASTA62569,707
        10         20         30         40         50         60 
SLTGVFPSGL IETKVSAAKI TENYQFDSRI RLNSIGFIPN HSKKATIAAN CSTFYVVKED 

        70         80         90        100        110        120 
GTIVYTGTAT SMFDNDTKET VYIADFSSVN EEGTYYLAVP GVGKSVNFKI AMNVYEDAFK 

       130        140        150        160        170        180 
TAMLGMYLLR CGTSVSATYN GIHYSHGPCH TNDAYLDYIN GQHTKKDSTK GWHDAGDYNK 

       190        200        210        220        230        240 
YVVNAGITVG SMFLAWEHFK DQLEPVALEI PEKNNSIPDF LDELKYEIDW ILTMQYPDGS 

       250        260        270        280        290        300 
GRVAHKVSTR NFGGFIMPEN EHDERFFVPW SSAATADFVA MTAMAARIFR PYDPQYAEKC 

       310        320        330        340        350        360 
INAAKVSYEF LKNNPANVFA NQSGFSTGEY ATVSDADDRL WAAAEMWETL GDEEYLRDFE 

       370        380        390        400        410        420 
NRAAQFSKKI EADFDWDNVA NLGMFTYLLS ERPGKNPALV QSIKDSLLST ADSIVRTSQN 

       430        440        450        460        470        480 
HGYGRTLGTT YYWGCNGTVV RQTMILQVAN KISPNNDYVN AALDAISHVF GRNYYNRSYV 

       490        500        510        520        530        540 
TGLGINPPMN PHDRRSGADG IWEPWPGYLV GGGWPGPKDW VDIQDSYQTN EIAINWNAAL 

       550        560        570        580        590        600 
IYALAGFVNY NSPQNEVLYG DVNDDGKVNS TDLTLLKRYV LKAVSTLPSS KAEKNADVNR 

       610        620 
DGRVNSSDVT ILSRYLIRVI EKLPI 

« Hide

References

[1]"Calcium-binding affinity and calcium-enhanced activity of Clostridium thermocellum endoglucanase D."
Chauvaux S., Beguin P., Aubert J.-P., Bhat K.M., Gow L.A., Wood T.M., Bairoch A.
Biochem. J. 265:261-265(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING DATA.
[2]"Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum."
Tomme P., Chauvaux S., Beguin P., Millet J., Aubert J.-P., Claeyssens M.
J. Biol. Chem. 266:10313-10318(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE HIS-492, MUTAGENESIS OF HISTIDINE RESIDUES.
[3]"Site-directed mutagenesis of essential carboxylic residues in Clostridium thermocellum endoglucanase CelD."
Chauvaux S., Beguin P., Aubert J.-P.
J. Biol. Chem. 267:4472-4478(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE GLU-531, MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES.
[4]"Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum."
Tomme P., van Beeumen J., Claeyssens M.
Biochem. J. 285:319-324(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE ASP-522.
[5]"Three-dimensional structure of a thermostable bacterial cellulase."
Juy M., Amit A.G., Alzari P.M., Poljak R.J., Claeyssens M., Beguin P., Aubert J.-P.
Nature 357:89-91(1992)
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[6]"Multiple crystal forms of endoglucanase CelD: signal peptide residues modulate lattice formation."
Chitarra V., Souchon H., Spinelli S., Juy M., Beguin P., Alzari P.M.
J. Mol. Biol. 248:225-232(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[7]"The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism."
Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M.
J. Mol. Biol. 257:1042-1051(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 AND 2.3 ANGSTROMS) OF MUTANT GLN-116.

Cross-references

Sequence databases

PIRCZCLDM. A25535.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLCX-ray1.90A1-625[»]
ProteinModelPortalP0C2S4.
SMRP0C2S4. Positions 11-551, 556-625.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceP0C2S4.

Entry information

Entry nameGUND_CLOTM
AccessionPrimary (citable) accession number: P0C2S4
Secondary accession number(s): P04954
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 36 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