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A2QYR9 (CBHC_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 37. 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:
Probable 1,4-beta-D-glucan cellobiohydrolase C

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C
Gene names
Name:cbhC
ORF Names:An12g02220
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

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

Subcellular location

Secreted By similarity.

Domain

Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similarities

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

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulose 1,4-beta-cellobiosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 459441Probable 1,4-beta-D-glucan cellobiohydrolase C
PRO_5000220698

Regions

Domain19 – 5436CBM1
Region54 – 9441Thr-rich linker
Region95 – 459365Catalytic

Sites

Active site1891 By similarity
Active site2351Proton donor By similarity
Active site4141Nucleophile By similarity

Amino acid modifications

Glycosylation3031N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 43 By similarity
Disulfide bond37 ↔ 53 By similarity
Disulfide bond190 ↔ 249 By similarity
Disulfide bond381 ↔ 428 By similarity

Sequences

Sequence LengthMass (Da)Tools
A2QYR9 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: A584E983E58DCE87

FASTA45948,126
        10         20         30         40         50         60 
MHYPLSLALA FLPFGIQAQQ TLWGQCGGQG YSGATSCVAG ATCATVNEYY AQCTPAAGTS 

        70         80         90        100        110        120 
SATTLKTTTS STTAAVTTTT TTQSPTGSAS PTTTASASGN PFSGYQLYVN PYYSSEVASL 

       130        140        150        160        170        180 
AIPSLTGSLS SLQAAATAAA KVPSFVWLDT AAKVPTMGDY LADIQSQNAA GANPPIAGQF 

       190        200        210        220        230        240 
VVYDLPDRDC AALASNGEYS IADNGVEHYK SYIDSIREIL VQYSDVHTLL VIEPDSLANL 

       250        260        270        280        290        300 
VTNLNVAKCA NAESAYLECT NYALTQLNLP NVAMYLDAGH AGWLGWPANQ QPAADLFASV 

       310        320        330        340        350        360 
YKNASSPAAV RGLATNVANY NAWTISSCPS YTQGNSVCDE QQYINAIAPL LQAQGFDAHF 

       370        380        390        400        410        420 
IVDTGRNGKQ PTGQQAWGDW CNVINTGFGE RPTTDTGDAL VDAFVWVKPG GESDGTSDSS 

       430        440        450 
ATRYDAHCGY SDALQPAPEA GTWFQAYFVQ LLTNANPAF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270264 Genomic DNA. Translation: CAK41068.1.
RefSeqXP_001395308.1. XM_001395271.2.

3D structure databases

ProteinModelPortalA2QYR9.
SMRA2QYR9. Positions 20-54, 94-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00009490.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00009671; CADANGAP00009490; CADANGAG00009671.
GeneID4985573.
KEGGang:ANI_1_300104.

Phylogenomic databases

eggNOGCOG5297.
HOGENOMHOG000178851.
OrthoDBEOG72C594.

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...

Entry information

Entry nameCBHC_ASPNC
AccessionPrimary (citable) accession number: A2QYR9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: March 6, 2007
Last modified: March 19, 2014
This is version 37 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