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A3DBX3 (GUB_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:
Beta-glucanase

EC=3.2.1.73
Alternative name(s):
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Endo-beta-1,3-1,4 glucanase
Laminarinase
Lichenase
Gene names
Name:licB
Synonyms:lam1
Ordered Locus Names:Cthe_0211
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

Subunit structure

May form part of a multienzyme complex (cellulosome) 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 16 family.

Ontologies

Keywords
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionlicheninase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 334307Beta-glucanase
PRO_0000284719

Regions

Repeat273 – 296241
Repeat308 – 331242
Region273 – 331592 X 24 AA approximate repeats
Compositional bias252 – 26918Pro/Thr-rich (linker)

Sites

Active site1361Nucleophile By similarity
Active site1401Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A3DBX3 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 0837564E9726F281

FASTA33437,897
        10         20         30         40         50         60 
MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE KADWANGSVF 

        70         80         90        100        110        120 
NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRTKSF FGYGYYEVRM KAAKNVGIVS 

       130        140        150        160        170        180 
SFFTYTGPSD NNPWDEIDIE FLGKDTTKVQ FNWYKNGVGG NEYLHNLGFD ASQDFHTYGF 

       190        200        210        220        230        240 
EWRPDYIDFY VDGKKVYRGT RNIPVTPGKI MMNLWPGIGV DEWLGRYDGR TPLQAEYEYV 

       250        260        270        280        290        300 
KYYPNGVPQD NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP 

       310        320        330 
VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the Clostridium thermocellum gene licB and the encoded beta-1,3-1,4-glucanase. A catalytic region homologous to Bacillus lichenases joined to the reiterated domain of clostridial cellulases."
Schimming S., Schwarz W.H., Staudenbauer W.L.
Eur. J. Biochem. 204:13-19(1992) [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63355 Genomic DNA. Translation: CAA44959.1.
CP000568 Genomic DNA. Translation: ABN51452.1.
PIRS23498.
RefSeqYP_001036645.1. NC_009012.1.

3D structure databases

ProteinModelPortalA3DBX3.
SMRA3DBX3. Positions 41-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_0211.

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN51452; ABN51452; Cthe_0211.
GeneID4808629.
KEGGcth:Cthe_0211.
PATRIC19514051. VBICloThe47081_0224.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2273.
HOGENOMHOG000250723.
OMATAPGEAC.
OrthoDBEOG6JB18P.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-216-MONOMER.
MetaCyc:MONOMER-16465.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
2.60.120.200. 1 hit.
InterProIPR008264. Beta_glucanase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamPF00404. Dockerin_1. 2 hits.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSPR00737. GLHYDRLASE16.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUB_CLOTH
AccessionPrimary (citable) accession number: A3DBX3
Secondary accession number(s): P29716, P37074
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 20, 2007
Last modified: February 19, 2014
This is version 44 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