Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5B2E8 (CBHC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 52. 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 C

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C
Gene names
Name:cbhC
ORF Names:AN5282
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Active against carboxymethylcellulose, beta-glucan and lichenan. Ref.1

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.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Ref.1

Temperature dependence:

Optimum temperature is 57 degrees Celsius.

Sequence caution

The sequence CBF82181.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA62442.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 4554361,4-beta-D-glucan cellobiohydrolase C
PRO_0000394053

Regions

Domain20 – 5536CBM1
Region59 – 9234Thr-rich linker
Region93 – 450358Catalytic

Sites

Active site1851 By similarity
Active site2311Proton donor By similarity
Active site4101Nucleophile By similarity

Amino acid modifications

Disulfide bond27 ↔ 44 By similarity
Disulfide bond38 ↔ 54 By similarity
Disulfide bond186 ↔ 245 By similarity
Disulfide bond377 ↔ 424 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5B2E8 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 32C2655B3E4CCA1F

FASTA45547,624
        10         20         30         40         50         60 
MHYSASGLAL AFLLPAIQAQ QTLYGQCGGS GWTGATSCVA GAACSTLNQW YAQCLPAATT 

        70         80         90        100        110        120 
TSTTLTTTTS SVTTTSNPGS TTTTSSVTVT ATASGNPFSG YQLYVNPYYS SEVQSIAIPS 

       130        140        150        160        170        180 
LTGTLSSLAP AATAAAKVPS FVWLDVAAKV PTMATYLADI RSQNAAGANP PIAGQFVVYD 

       190        200        210        220        230        240 
LPDRDCAALA SNGEFAISDG GVQHYKDYID SIREILVEYS DVHVILVIEP DSLANLVTNL 

       250        260        270        280        290        300 
NVAKCANAQS AYLECTNYAV TQLNLPNVAM YLDAGHAGWL GWPANLQPAA NLYAGVYSDA 

       310        320        330        340        350        360 
GSPAALRGLA TNVANYNAWA IDTCPSYTQG NSVCDEKDYI NALAPLLRAQ GFDAHFITDT 

       370        380        390        400        410        420 
GRNGKQPTGQ QAWGDWCNVI GTGFGARPST NTGDSLLDAF VWVKPGGESD GTSDTSAARY 

       430        440        450 
DAHCGYSDAL QPAPEAGTWF QAYFVQLLQN ANPSF 

« Hide

References

« Hide 'large scale' references
[1]"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490497 mRNA. Translation: ABF50873.1.
AACD01000093 Genomic DNA. Translation: EAA62442.1. Sequence problems.
BN001305 Genomic DNA. Translation: CBF82181.1. Sequence problems.
RefSeqXP_662886.1. XM_657794.1.

3D structure databases

ProteinModelPortalQ5B2E8.
SMRQ5B2E8. Positions 21-55, 90-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00003822.

Protein family/group databases

mycoCLAPCBH6C_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003822; CADANIAP00003822; CADANIAG00003822.
GeneID2871574.
KEGGani:AN5282.2.

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_EMENI
AccessionPrimary (citable) accession number: Q5B2E8
Secondary accession number(s): C8VH03, Q1HFS7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: March 19, 2014
This is version 52 of the entry and version 2 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