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A2QAI7 (CBHB_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 39. 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 B

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B
Gene names
Name:cbhB
ORF Names:An01g11660
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length536 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 Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) 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 – 2121 Potential
Chain22 – 536515Probable 1,4-beta-D-glucan cellobiohydrolase B
PRO_5000219450

Regions

Domain500 – 53637CBM1
Region22 – 458437Catalytic
Region459 – 50042Ser/Thr-rich linker

Sites

Active site2331Nucleophile By similarity
Active site2381Proton donor By similarity

Amino acid modifications

Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Disulfide bond508 ↔ 525 By similarity
Disulfide bond519 ↔ 535 By similarity

Sequences

Sequence LengthMass (Da)Tools
A2QAI7 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: EB9040AC12C8EA60

FASTA53656,205
        10         20         30         40         50         60 
MSSFQVYRAA LLLSILATAN AQQVGTYTTE THPSLTWQTC TSDGSCTTND GEVVIDANWR 

        70         80         90        100        110        120 
WVHSTSSATN CYTGNEWDTS ICTDDVTCAA NCALDGATYE ATYGVTTSGS ELRLNFVTQG 

       130        140        150        160        170        180 
SSKNIGSRLY LMSDDSNYEL FKLLGQEFTF DVDVSNLPCG LNGALYFVAM DADGGTSEYS 

       190        200        210        220        230        240 
GNKAGAKYGT GYCDSQCPRD LKFINGEANC DGWEPSSNNV NTGVGDHGSC CAEMDVWEAN 

       250        260        270        280        290        300 
SISNAFTAHP CDSVSQTMCD GDSCGGTYSA SGDRYSGTCD PDGCDYNPYR LGNTDFYGPG 

       310        320        330        340        350        360 
LTVDTNSPFT VVTQFITDDG TSSGTLTEIK RLYVQNGEVI ANGASTYSSV NGSSITSAFC 

       370        380        390        400        410        420 
ESEKTLFGDE NVFDKHGGLE GMGEAMAKGM VLVLSLWDDY AADMLWLDSD YPVNSSASTP 

       430        440        450        460        470        480 
GVARGTCSTD SGVPATVEAE SPNAYVTYSN IKFGPIGSTY SSGSSSGSGS SSSSSSTTTK 

       490        500        510        520        530 
ATSTTLKTTS TTSSGSSSTS AAQAYGQCGG QGWTGPTTCV SGYTCTYENA YYSQCL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM269981 Genomic DNA. Translation: CAK44068.1.
RefSeqXP_001389576.1. XM_001389539.2.

3D structure databases

ProteinModelPortalA2QAI7.
SMRA2QAI7. Positions 22-461, 502-536.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00001127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00001164; CADANGAP00001127; CADANGAG00001164.
GeneID4977345.
KEGGang:ANI_1_1574014.

Phylogenomic databases

HOGENOMHOG000182210.
KOK01225.
OrthoDBEOG7ZGXCF.

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_ASPNC
AccessionPrimary (citable) accession number: A2QAI7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: March 6, 2007
Last modified: November 13, 2013
This is version 39 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