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Q84C00 (GUB_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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).

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 16 family.

Ontologies

Keywords
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
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_0000011792

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

Experimental info

Sequence conflict971S → T in CAA41281. Ref.1
Sequence conflict971S → T Ref.2
Sequence conflict1491A → V in CAA41281. Ref.1
Sequence conflict1491A → V Ref.2
Sequence conflict1571E → G in CAA41281. Ref.1
Sequence conflict1571E → G Ref.2
Sequence conflict2181K → I in CAA41281. Ref.1
Sequence conflict2181K → I Ref.2
Sequence conflict304 – 33431QSVAD…AIPSL → PQDGCGRHDRVVDSGSK in CAA41281. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q84C00 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3079DEF1CEE5A664

FASTA33437,942
        10         20         30         40         50         60 
MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE KADWANGSVF 

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

       130        140        150        160        170        180 
SFFTYTGPSD NNPWDEIDIE FLGKDTTKAQ FNWYKNEVGG NEYLHNLGFD ASQDFHTYGF 

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

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

       310        320        330 
VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL 

« Hide

References

[1]"Nucleotide sequence of the Clostridium thermocellum laminarinase gene."
Zverlov V.V., Laptev D.A., Tishkov V.I., Velikodvorskaja G.A.
Biochem. Biophys. Res. Commun. 181:507-512(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: F7.
[2]Zverlov V.V.
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Lv W.-P., Xu Z.-R., Li W.-F., Sun J.-Y., Xu Y.-X., Gu S.-H.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning the Clostridium thermocellum thermostable laminarinase gene in Escherichia coli; the properties of the enzyme thus produced."
Zverlov V.V., Velikodvorskaja G.A.
Biotechnol. Lett. 12:811-816(1990)
Cited for: CHARACTERIZATION.
Strain: F7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58392 Genomic DNA. Translation: CAA41281.1.
AY225318 Genomic DNA. Translation: AAO74890.1.
PIRJS0611.

3D structure databases

ProteinModelPortalQ84C00.
SMRQ84C00. Positions 33-246.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_CLOTM
AccessionPrimary (citable) accession number: Q84C00
Secondary accession number(s): P29716, P37074
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 53 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