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P17901 (GUNA_CLOCE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 111. 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

EC=3.2.1.4
Alternative name(s):
Cellulase A
EGCCA
Endo-1,4-beta-glucanase A
Gene names
Name:celCCA
Ordered Locus Names:Ccel_1099
OrganismClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]
Taxonomic identifier394503 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

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.

Miscellaneous

The C-terminus (AA 411-475) may play a role in organizing the cellulosome complex.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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 – 2626 Ref.1
Chain27 – 475449Endoglucanase A
PRO_0000007845

Regions

Repeat415 – 438241
Repeat446 – 469242
Region415 – 469552 X 24 AA approximate repeats

Sites

Active site1471 Probable
Active site1951Proton donor
Active site3321Nucleophile

Experimental info

Mutagenesis1041R → K: Small loss of activity. Ref.4
Mutagenesis1041R → S or V: Large decrease of activity. Ref.4
Mutagenesis1471H → S, E, G or F: Total loss of activity. Ref.4
Mutagenesis1481H → V: Large decrease of activity. Ref.4

Secondary structure

......................................................................... 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17901 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 1AF20EA2C0A132F9

FASTA47553,625
        10         20         30         40         50         60 
MKKTTAFLLC FLMIFTALLP MQNANAYDAS LIPNLQIPQK NIPNNDGMNF VKGLRLGWNL 

        70         80         90        100        110        120 
GNTFDAFNGT NITNELDYET SWSGIKTTKQ MIDAIKQKGF NTVRIPVSWH PHVSGSDYKI 

       130        140        150        160        170        180 
SDVWMNRVQE VVNYCIDNKM YVILNTHHDV DKVKGYFPSS QYMASSKKYI TSVWAQIAAR 

       190        200        210        220        230        240 
FANYDEHLIF EGMNEPRLVG HANEWWPELT NSDVVDSINC INQLNQDFVN TVRATGGKNA 

       250        260        270        280        290        300 
SRYLMCPGYV ASPDGATNDY FRMPNDISGN NNKIIVSVHA YCPWNFAGLA MADGGTNAWN 

       310        320        330        340        350        360 
INDSKDQSEV TWFMDNIYNK YTSRGIPVII GECGAVDKNN LKTRVEYMSY YVAQAKARGI 

       370        380        390        400        410        420 
LCILWDNNNF SGTGELFGFF DRRSCQFKFP EIIDGMVKYA FEAKTDPDPV IVYGDYNNDG 

       430        440        450        460        470 
NVDALDFAGL KKYIMAADHA YVKNLDVNLD NEVNAFDLAI LKKYLLGMVS KLPSN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Clostridium cellulolyticum endoglucanase-A-encoding gene, celCCA."
Faure E., Belaich A., Bagnara C., Gaudin C., Belaich J.-P.
Gene 84:39-46(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-39.
[2]"Complete sequence of Clostridium cellulolyticum H10."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ivanova N., Zhou J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
[3]"Characterization of endoglucanase A from Clostridium cellulolyticum."
Fierobe H.-P., Gaudin C., Belaich A., Loufti M., Faure E., Bagnara C., Baty D., Belaich J.-P.
J. Bacteriol. 173:7956-7962(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"The catalytic domain of endoglucanase A from Clostridium cellulolyticum: effects of arginine 79 and histidine 122 mutations on catalysis."
Belaich A., Fierobe H.-P., Baty D., Busetta B., Bagnara-Tardif C., Gaudin C., Belaich J.-P.
J. Bacteriol. 174:4677-4682(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-104; HIS-147 AND HIS-148.
[5]"Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5."
Ducros V., Czjzek M., Belaich A., Gaudin C., Fierobe H.P., Belaich J.-P., Davies G.J., Haser R.
Structure 3:939-949(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 27-406.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93096 Genomic DNA. Translation: AAA51444.1.
M32362 Genomic DNA. Translation: AAA23221.1.
CP001348 Genomic DNA. Translation: ACL75458.1.
RefSeqYP_002505438.1. NC_011898.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EDGX-ray1.60A27-401[»]
2VN5X-ray1.90B/D410-475[»]
2VN6X-ray1.49B410-472[»]
ProteinModelPortalP17901.
SMRP17901. Positions 27-401, 410-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394503.Ccel_1099.

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL75458; ACL75458; Ccel_1099.
GeneID7309912.
KEGGcce:Ccel_1099.
PATRIC19433019. VBICloCel57783_1132.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000027405.
KOK01179.
OMATWGEEAT.
OrthoDBEOG6KHFWF.

Enzyme and pathway databases

BioCycCCEL394503:GJET-1124-MONOMER.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
3.20.20.80. 1 hit.
InterProIPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
PF00404. Dockerin_1. 2 hits.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17901.

Entry information

Entry nameGUNA_CLOCE
AccessionPrimary (citable) accession number: P17901
Secondary accession number(s): B8HZV8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 14, 2014
This is version 111 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