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Q9UVS9 (CBHA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 54. 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 A

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase A
Cellobiohydrolase D
Exocellobiohydrolase A
Exoglucanase A
Gene names
Name:cbhA
Synonyms:celD
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length452 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.3

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.

Induction

Expression is under the control of the xylanolytic transcriptional activator xlnR. Ref.1 Ref.3

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 4524351,4-beta-D-glucan cellobiohydrolase A
PRO_5000056394

Sites

Active site2271Nucleophile By similarity
Active site2321Proton donor By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1011V → I in ACT65727. Ref.2
Sequence conflict1701V → A in ACT65727. Ref.2
Sequence conflict3591E → D in ACT65727. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UVS9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6364A0F4BF7D254F

FASTA45248,258
        10         20         30         40         50         60 
MHQRALLFSA LLTAVRAQQA GTLTEEVHPS LTWQKCTSEG SCTEQSGSVV IDSNWRWTHS 

        70         80         90        100        110        120 
VNDSTNCYTG NTWDATLCPD DETCAANCAL DGADYESTYG VTTDGDSLTL KFVTGSNVGS 

       130        140        150        160        170        180 
RLYLMDTSDE GYQTFNLLDA EFTFDVDVSN LPCGLNGALY FTAMDADGGV SKYPANKAGA 

       190        200        210        220        230        240 
KYGTGYCDSQ CPRDLKFIDG QANVDGWEPS SNNDNTGIGN HGSCCPEMDI WEANKISTAL 

       250        260        270        280        290        300 
TPHPCDSSEQ TMCEGNDCGG TYSDDRYGGT CDPDGCDFNP YRMGNDSFYG PGKTIDTGSK 

       310        320        330        340        350        360 
MTVVTQFITD GSGSLSEIKR YYVQNGNVIA NADSNISGVT GNSITTDFCT AQKKAFGDED 

       370        380        390        400        410        420 
IFAEHNGLAG ISDAMSSMVL ILSLWDDYYA SMEWLDSDYP ENATATDPGV ARGTCDSESG 

       430        440        450 
VPATVEGAHP DSSVTFSNIK FGPINSTFSA SA 

« Hide

References

[1]"Two cellobiohydrolase-encoding genes from Aspergillus niger require D-xylose and the xylanolytic transcriptional activator XlnR for their expression."
Gielkens M.M., Dekkers E., Visser J., de Graaff L.H.
Appl. Environ. Microbiol. 65:4340-4345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]Hsing-Ren W., Trong-Rong Y.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BCRC 31494.
[3]"Induction, production, repression, and de-repression of exoglucanase synthesis in Aspergillus niger."
Hanif A., Yasmeen A., Rajoka M.I.
Bioresour. Technol. 94:311-319(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF156268 Genomic DNA. Translation: AAF04491.1.
GQ281319 Genomic DNA. Translation: ACT65727.1.

3D structure databases

ProteinModelPortalQ9UVS9.
SMRQ9UVS9. Positions 18-449.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPCBH7A_ASPNG.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG85664.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCBHA_ASPNG
AccessionPrimary (citable) accession number: Q9UVS9
Secondary accession number(s): C7ENW1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: May 1, 2000
Last modified: November 13, 2013
This is version 54 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