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Q7SIG5 (GUN6_HUMIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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-6B

EC=3.2.1.4
Alternative name(s):
Cellulase 6B
Endo-1,4-beta-glucanase 6B
Gene names
Name:cel6B
OrganismHumicola insolens (Soft-rot fungus)
Taxonomic identifier34413 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a central role in the recycling of plant biomass. 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. Ref.1

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 6 (cellulase B) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
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

Chain1 – 348348Endoglucanase-6B
PRO_0000248842

Sites

Active site921Proton donor Potential Ref.2
Active site1391Proton donor Ref.2
Binding site521Substrate By similarity UniProtKB Q9C1S9
Binding site541Substrate By similarity UniProtKB Q9C1S9
Binding site1831Substrate By similarity UniProtKB Q9C1S9
Binding site1861Substrate By similarity UniProtKB Q9C1S9
Binding site2221Substrate By similarity UniProtKB Q9C1S9
Binding site2821Substrate By similarity UniProtKB Q9C1S9
Binding site3101Substrate By similarity UniProtKB Q9C1S9
Binding site3141Substrate By similarity UniProtKB Q9C1S9

Secondary structure

........................................................... 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7SIG5 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 5F1E4A4367402E54

FASTA34837,753
        10         20         30         40         50         60 
QSGNPFSGRT LLVNSDYSSK LDQTRQAFLS RGDQTNAAKV KYVQEKVGTF YWISNIFLLR 

        70         80         90        100        110        120 
DIDVAIQNAR AAKARGENPI VGLVLYNLPD RDCSAGESSG ELKLSQNGLN RYKNEYVNPF 

       130        140        150        160        170        180 
AQKLKAASDV QFAVILEPDA IGNMVTGTSA FCRNARGPQQ EAIGYAISQL QASHIHLYLD 

       190        200        210        220        230        240 
VANGGWLGWA DKLEPTAQEV ATILQKAGNN AKIRGFSSNV SNYNPYSTSN PPPYTSGSPS 

       250        260        270        280        290        300 
PDESRYATNI ANAMRQRGLP TQFIIDQSRV ALSGARSEWG QWCNVNPAGF GQPFTTNTNN 

       310        320        330        340 
PNVDAIVWVK PGGESDGQCG MGGAPAAGMW FDAYAQMLTQ NAHDEIAR 

« Hide

References

[1]"Enzymatic properties of cellulases from Humicola insolens."
Schuelein M.
J. Biotechnol. 57:71-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[2]"Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution."
Davies G.J., Brzozowski A.M., Dauter M., Varrot A., Schuelein M.
Biochem. J. 348:201-207(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, ACTIVE SITE.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYSX-ray1.60A/B1-348[»]
ProteinModelPortalQ7SIG5.
SMRQ7SIG5. Positions 3-347.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH6. Glycoside Hydrolase Family 6.
mycoCLAPEGL6B_HUMIN.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17625.

Family and domain databases

Gene3D3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamPF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSPR00733. GLHYDRLASE6.
SUPFAMSSF51989. SSF51989. 1 hit.
PROSITEPS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7SIG5.

Entry information

Entry nameGUN6_HUMIN
AccessionPrimary (citable) accession number: Q7SIG5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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