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O59843 (CBHB_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 74. 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:
1,4-beta-D-glucan cellobiohydrolase B

EC=3.2.1.91
Alternative name(s):
1,4-beta-D-glucan cellobiohydrolase I
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B
Gene names
Name:cbhB
Synonyms:cbhI
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.2

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) family.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 5405181,4-beta-D-glucan cellobiohydrolase B
PRO_0000007918

Regions

Domain505 – 54036CBM1
Region23 – 459437Catalytic
Region460 – 50546Ser/Thr-rich linker

Sites

Active site2341Nucleophile By similarity
Active site2391Proton donor By similarity

Amino acid modifications

Glycosylation4341N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Disulfide bond513 ↔ 529 By similarity
Disulfide bond524 ↔ 539 By similarity

Sequences

Sequence LengthMass (Da)Tools
O59843 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 002D7FD28DF194D0

FASTA54057,099
        10         20         30         40         50         60 
MVDSFSIYKT ALLLSMLATS NAQQVGTYTA ETHPSLTWQT CSGSGSCTTT SGSVVIDANW 

        70         80         90        100        110        120 
RWVHEVGGYT NCYSGNTWDS SICSTDTTCA SECALEGATY ESTYGVTTSG SSLRLNFVTT 

       130        140        150        160        170        180 
ASQKNIGSRL YLLADDSTYE TFKLFNREFT FDVDVSNLPC GLNGALYFVS MDADGGVSRF 

       190        200        210        220        230        240 
PTNKAGAKYG TGYCDSQCPR DLKFIDGQAN IEGWEPSSTD VNAGTGNHGS CCPEMDIWEA 

       250        260        270        280        290        300 
NSISSAFTAH PCDSVQQTMC TGDTCGGTYS DTTDRYSGTC DPDGCDFNPY RFGNTNFYGP 

       310        320        330        340        350        360 
GKTVDNSKPF TVVTQFITHD GTDTGTLTEI RRLYVQNGVV IGNGPSTYTA ASGNSITESF 

       370        380        390        400        410        420 
CKAEKTLFGD TNVFETHGGL SAMGDALGDG MVLVLSLWDD HAADMLWLDS DYPTTSCASS 

       430        440        450        460        470        480 
PGVARGTCPT TTGNATYVEA NYPNSYVTYS NIKFGTLNST YSGTSSGGSS SSSTTLTTKA 

       490        500        510        520        530        540 
STSTTSSKTT TTTSKTSTTS SSSTNVAQLY GQCGGQGWTG PTTCASGTCT KQNDYYSQCL 

« Hide

References

[1]"Cloning, nucleotide sequence, and transcriptional analysis of Aspergillus aculeatus No.F-50 cellobiohydrolase I (cbhI) gene."
Takada G., Kawaguchi T., Sumitani J., Arai M.
J. Ferment. Bioeng. 85:1-9(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: F-50.
[2]"Overexpression of Aspergillus aculeatus cellobiohydrolase I in Aspergillus oryzae."
Kanamasa S., Mochizuki M., Takada G., Kawaguchi T., Sumitani J., Araii M.
J. Biosci. Bioeng. 95:627-629(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002821 mRNA. Translation: BAA25183.1.

3D structure databases

ProteinModelPortalO59843.
SMRO59843. Positions 23-462, 507-540.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPCBH7A_ASPAC.

Proteomic databases

PRIDEO59843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBHB_ASPAC
AccessionPrimary (citable) accession number: O59843
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: November 13, 2013
This is version 74 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries