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Q5B2Q4 (CBHA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 61. 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 A

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase A
Cellobiohydrolase D
Exocellobiohydrolase A
Exoglucanase A
Gene names
Name:cbhA
Synonyms:celD
ORF Names:AN5176
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 length446 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 By similarity. 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.

Subcellular location

Secreted Probable.

Induction

Repressed by D-glucose. Ref.1

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
   Technical termComplete proteome
Reference 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 446429Probable 1,4-beta-D-glucan cellobiohydrolase A
PRO_0000393544

Sites

Active site2261Nucleophile By similarity
Active site2311Proton donor By similarity

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation2841N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1501L → F in AAM54069. Ref.1
Sequence conflict2861S → R in AAM54069. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5B2Q4 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: DACEE446E809A6D2

FASTA44647,638
        10         20         30         40         50         60 
MYQRALLFSA LLSVSRAQQA GTAQEEVHPS LTWQRCEASG SCTEVAGSVV LDSNWRWTHS 

        70         80         90        100        110        120 
VDGYTNCYTG NEWDATLCPD NESCAQNCAV DGADYEATYG ITSNGDSLTL KFVTGSNVGS 

       130        140        150        160        170        180 
RVYLMEDDET YQMFDLLNNE FTFDVDVSNL PCGLNGALYF TSMDADGGLS KYEGNTAGAK 

       190        200        210        220        230        240 
YGTGYCDSQC PRDIKFINGL GNVEGWEPSD SDANAGVGGM GTCCPEMDIW EANSISTAYT 

       250        260        270        280        290        300 
PHPCDSVEQT MCEGDSCGGT YSDDRYGGTC DPDGCDFNSY RMGNTSFYGP GAIIDTSSKF 

       310        320        330        340        350        360 
TVVTQFIADG GSLSEIKRFY VQNGEVIPNS ESNISGVEGN SITSEFCTAQ KTAFGDEDIF 

       370        380        390        400        410        420 
AQHGGLSAMG DAASAMVLIL SIWDDHHSSM MWLDSSYPTD ADPSQPGVAR GTCEQGAGDP 

       430        440 
DVVESEHADA SVTFSNIKFG PIGSTF 

« Hide

References

« Hide 'large scale' references
[1]"Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans."
Lockington R.A., Rodbourn L., Barnett S., Carter C.J., Kelly J.M.
Fungal Genet. Biol. 37:190-196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
[2]"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.
[3]"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.
[4]"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
AF420019 Genomic DNA. Translation: AAM54069.1.
DQ490495 mRNA. Translation: ABF50871.1.
AACD01000089 Genomic DNA. Translation: EAA62357.1.
BN001305 Genomic DNA. Translation: CBF81021.1.
RefSeqXP_662780.1. XM_657688.1.

3D structure databases

ProteinModelPortalQ5B2Q4.
SMRQ5B2Q4. Positions 18-446.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPCBH7A_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003171; CADANIAP00003171; CADANIAG00003171.
GeneID2871468.
KEGGani:AN5176.2.

Phylogenomic databases

eggNOGNOG85664.
HOGENOMHOG000182210.
OMANWSKCTS.
OrthoDBEOG7ZGXCF.

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_EMENI
AccessionPrimary (citable) accession number: Q5B2Q4
Secondary accession number(s): C8VF49, Q1HFS9, Q8NK03
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: January 22, 2014
This is version 61 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