Endoglucanase D precursor - Clostridium thermocellum (strain ATCC 27405 / DSM 1237)

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A3DDN1 (GUND_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Clostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]

Taxonomic identifier

203119 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length	649 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 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 process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 41

By similarity

Chain

42 – 649

608

Endoglucanase D

PRO_0000284722

Regions

Repeat

585 – 608

Repeat

621 – 644

Region

585 – 644

2 X 24 AA approximate repeats

Sites

Active site

201

Nucleophile By similarity

Active site

516

By similarity

Active site

546

By similarity

Active site

555

Proton donor By similarity

Experimental info

Sequence conflict

577

A → P in CAA28255. Ref.1

Secondary structure

649

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

A3DDN1 [UniParc].

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

FASTA

649

72,415

        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' referencesShow '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. 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.

PIR

CZCLDM. A25535.

RefSeq

YP_001037253.1. NC_009012.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4FL4	X-ray	2.90	A/D/G/J	584-649	[»]

ProteinModelPortal

A3DDN1.

SMR

A3DDN1. Positions 35-575, 580-649.

ModBase

Search...

Protein-protein interaction databases

STRING

203119.Cthe_0825.

Protein family/group databases

CAZy

GH9. Glycoside Hydrolase Family 9.

Proteomic databases

PRIDE

A3DDN1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ABN52060; ABN52060; Cthe_0825.

GeneID

4810443.

KEGG

cth:Cthe_0825.

PATRIC

19515357. VBICloThe47081_0867.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

NOG05134.

HOGENOM

HOG000245359.

K01179.

OMA

CSYASNE.

ProtClustDB

CLSK2471711.

Enzyme and pathway databases

BioCyc

CTHE203119:GIW8-854-MONOMER.
MetaCyc:MONOMER-16416.

Family and domain databases

Gene3D

1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.40.10. 1 hit.

InterPro

IPR008928. 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]

Pfam

PF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]

SUPFAM

SSF63446. Cellulos_enz_dockerin_1. 1 hit.
SSF48208. Glyco_trans_6hp. 1 hit.
SSF81296. Ig_E-set. 1 hit.

PROSITE

PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits. Uncertain.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

A3DDN1.

Entry information

Entry name

GUND_CLOTH

Accession

Primary (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 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents