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Q9C1S9 (GUX6_HUMIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. 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:
Exoglucanase-6A

EC=3.2.1.91
Alternative name(s):
1,4-beta-cellobiohydrolase 6A
Avicelase 2
Beta-glucancellobiohydrolase 6A
Exocellobiohydrolase 6A
Gene names
Name:cel6A
Synonyms:avi2
OrganismHumicola insolens (Soft-rot fungus)
Taxonomic identifier34413 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.6

Catalytic activity

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains. Ref.2

Subunit structure

Monomer. Ref.3 Ref.4 Ref.5 Ref.6

Sequence similarities

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

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 476460Exoglucanase-6A
PRO_0000248843

Regions

Domain33 – 6028CBM1
Region200 – 22223Substrate binding loop 1 Ref.3 Ref.4 Ref.5
Region423 – 46139Substrate binding loop 2 Ref.3 Ref.4 Ref.5
Compositional bias73 – 786Poly-Ser

Sites

Active site2521Proton donor Ref.3 Ref.5
Active site4311Proton acceptor Probable Ref.3 Ref.4 Ref.5
Binding site1631Substrate Ref.3 Ref.4 Ref.5
Binding site1651Substrate Ref.3 Ref.4 Ref.5
Binding site2971Substrate Ref.3 Ref.4 Ref.5
Binding site3001Substrate Ref.3 Ref.4 Ref.5
Binding site3361Substrate Ref.3 Ref.4 Ref.5
Binding site3971Substrate Ref.3 Ref.4 Ref.5
Binding site4251Substrate Ref.3 Ref.4 Ref.5
Binding site4291Substrate Ref.3 Ref.4 Ref.5

Amino acid modifications

Glycosylation1441O-linked (Man...) Ref.6
Glycosylation1531O-linked (Man...) Ref.6
Glycosylation1671N-linked (GlcNAc...) Ref.3 Ref.4 Ref.5 Ref.6
Disulfide bond33 ↔ 50
Disulfide bond44 ↔ 60

Secondary structure

....................................................... 476
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9C1S9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D2B0054F1381E653

FASTA47651,276
        10         20         30         40         50         60 
MAKFFLTAAF AAAALAAPVV EERQNCAPTW GQCGGIGFNG PTCCQSGSTC VKQNDWYSQC 

        70         80         90        100        110        120 
LPGSQVTTTS TTSTSSSSTT SRATSTTRTG GVTSITTAPT RTVTIPGGAT TTASYNGNPF 

       130        140        150        160        170        180 
EGVQLWANNY YRSEVHTLAI PQITDPALRA AASAVAEVPS FQWLDRNVTV DTLLVETLSE 

       190        200        210        220        230        240 
IRAANQAGAN PPYAAQIVVY DLPDRDCAAA ASNGEWAIAN NGANNYKGYI NRIREILISF 

       250        260        270        280        290        300 
SDVRTILVIE PDSLANMVTN MNVAKCSGAA STYRELTIYA LKQLDLPHVA MYMDAGHAGW 

       310        320        330        340        350        360 
LGWPANIQPA AELFAKIYED AGKPRAVRGL ATNVANYNAW SISSPPPYTS PNPNYDEKHY 

       370        380        390        400        410        420 
IEAFRPLLEA RGFPAQFIVD QGRSGKQPTG QKEWGHWCNA IGTGFGMRPT ANTGHQYVDA 

       430        440        450        460        470 
FVWVKPGGEC DGTSDTTAAR YDYHCGLEDA LKPAPEAGQW FQAYFEQLLR NANPPF 

« Hide

References

[1]"Cloning and overexpression of the avi2 gene encoding a major cellulase produced by Humicola insolens FERM BP-5977."
Moriya T., Watanabe M., Sumida N., Okakura K., Murakami T.
Biosci. Biotechnol. Biochem. 67:1434-1437(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FERM BP-5977.
[2]"Enzymatic properties of cellulases from Humicola insolens."
Schuelein M.
J. Biotechnol. 57:71-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[3]"Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding."
Varrot A., Schuelein M., Davies G.J.
Biochemistry 38:8884-8891(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 115-476 IN COMPLEX WITH GLUCOSE AND CELLOTETRAOSE, ACTIVE SITE, GLYCOSYLATION AT ASN-167.
[4]"Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-beta-cellobioside, at 1.9 A."
Varrot A., Frandsen T.P., Driguez H., Davies G.J.
Acta Crystallogr. D 58:2201-2204(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-476 OF MUTANT ALA-416 IN COMPLEX WITH SUBSTRATE ANALOG, GLYCOSYLATION AT ASN-167.
[5]"Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens."
Varrot A., Frandsen T.P., von Ossowski I., Boyer V., Cottaz S., Driguez H., Schuelein M., Davies G.J.
Structure 11:855-864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 113-476 OF MUTANT ASN-431 IN COMPLEX WITH SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-167.
[6]"Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution."
Varrot A., Hastrup S., Schuelein M., Davies G.J.
Biochem. J. 337:297-304(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-476, FUNCTION, SUBUNIT, GLYCOSYLATION AT THR-144; SER-153 AND ASN-167.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB048710 Genomic DNA. Translation: BAB39154.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVWX-ray1.92A117-476[»]
1GZ1X-ray1.90A115-476[»]
1OC5X-ray1.70A113-476[»]
1OC6X-ray1.50A113-476[»]
1OC7X-ray1.11A113-476[»]
1OCBX-ray1.75A/B115-476[»]
1OCJX-ray1.30A115-476[»]
1OCNX-ray1.31A115-476[»]
2BVWX-ray1.70A/B115-476[»]
4I5RX-ray1.50A117-157[»]
4I5UX-ray1.22A117-161[»]
ProteinModelPortalQ9C1S9.
SMRQ9C1S9. Positions 30-61, 116-476.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPCBH6A_HUMIN.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSPR00733. GLHYDRLASE6.
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9C1S9.

Entry information

Entry nameGUX6_HUMIN
AccessionPrimary (citable) accession number: Q9C1S9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 58 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