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P28621 (GUNB_CLOC7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 B

EC=3.2.1.4
Alternative name(s):
Cellulase B
Endo-1,4-beta-glucanase B
Gene names
Name:engB
Ordered Locus Names:Clocel_1150
OrganismClostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) [Complete proteome] [HAMAP]
Taxonomic identifier573061 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Has endoglucanase activity on carboxymethyl-cellulose (CMC), xylan and lichenan, but not Avicel.

Catalytic activity

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

Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.

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

Up to 32 AA of the N-terminus and 52 AA of the C-terminus are not required for catalytic activity.

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 termComplete 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 – 3333 Potential
Chain34 – 440407Endoglucanase B
PRO_0000007847

Regions

Repeat387 – 410241
Repeat419 – 440222
Region387 – 440542 X 24 AA approximate repeats

Sites

Active site1791Proton donor By similarity
Active site3051Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P28621 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 93D6CB9EA7E2AF21

FASTA44048,637
        10         20         30         40         50         60 
MNKRLSRGKI SLLASVFVTT TFMGGVNVLA STAKTGIRDI TSQQVVKEMK VGWNLGNTMD 

        70         80         90        100        110        120 
ATGGETNWGN PLTTHAMIDK VKAAGFNTLR LPITWDGHIG AAPDYAIDAT WMNRVEEIAN 

       130        140        150        160        170        180 
YAFDNNMYVI INLHHEDGWL KPYYANEAEV KAKITKVWTQ IANRFKDYGD YLIFETMNEP 

       190        200        210        220        230        240 
RPVGAADEWS GGSYENRDMV NRYNLTAVNT IRATGGNNAL RHIMVPTLAA AALSTTMNDY 

       250        260        270        280        290        300 
IVPNNDSRVI VSLHMYSPYF FSADLTSQWT TATWGSDADK AALSADFDAV YNKFVKNGRA 

       310        320        330        340        350        360 
VVIGEMGTIN KNNLDSRVKH AEYYAKEATV RGITPIWWDN GYCVAGKEQT FGIFNRKNLT 

       370        380        390        400        410        420 
WCCPEVMQAF IRGAGATQTQ TSYSLGDVNK DGKVNAIDYA VLKSILLGTN TNVDLSVSDM 

       430        440 
NKDGKVNALD LAVLKKMLLS 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and characteristics of endoglucanase gene engB from Clostridium cellulovorans."
Foong F., Hamamoto T., Shoseyov O., Doi R.H.
J. Gen. Microbiol. 137:1729-1736(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Clostridium cellulovorans 743B."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Hemme C.L., Woyke T.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35296 / DSM 3052 / OCM 3 / 743B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M75706 Genomic DNA. Translation: AAA23231.1.
CP002160 Genomic DNA. Translation: ADL50906.1.
PIRA44815.
RefSeqYP_003842670.1. NC_014393.1.

3D structure databases

ProteinModelPortalP28621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28621. 1 interaction.

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL50906; ADL50906; Clocel_1150.
GeneID9607996.
KEGGccb:Clocel_1150.
PATRIC41738611. VBICloCel81632203721_3056.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000027405.
KOK01179.
OMARFKDYGD.

Enzyme and pathway databases

BioCycCCEL573061:GIXD-1188-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. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNB_CLOC7
AccessionPrimary (citable) accession number: P28621
Secondary accession number(s): D9SUK1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 14, 2014
This is version 85 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries