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Q00548 (GUX1_CRYPA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 70. 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:
Exoglucanase 1

EC=3.2.1.91
Alternative name(s):
1,4-beta-cellobiohydrolase I
Beta-glucancellobiohydrolase I
Exocellobiohydrolase I
Exoglucanase I
Gene names
Name:CBH-1
OrganismCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifier5116 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

Protein attributes

Sequence length452 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.

Catalytic activity

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

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 1818 Potential
Chain19 – 452434Exoglucanase 1
PRO_0000007920

Sites

Active site2301Nucleophile By similarity
Active site2351Proton donor By similarity

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q00548 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5802FD112C2CA864

FASTA45248,358
        10         20         30         40         50         60 
MFSKFALTGS LLAGAVNAQG VGTQQTETHP QMTWQSCTSP SSCTTNQGEV VIDSNWRWVH 

        70         80         90        100        110        120 
DKDGYVNCYT GNTWNTTLCP DDKTCAANCV LDGADYSSTY GITTSGNALS LQFVTQSSGK 

       130        140        150        160        170        180 
NIGSRTYLME SSTKYHLFDL IGNEFAFDVD LSKLPCGLNG ALYFVTMDAD GGMAKYSTNT 

       190        200        210        220        230        240 
AGAEYGTGYC DSQCPRDLKF INGQGNVEGW TPSTNDANAG VGGLGSCCSE MDVWEANSMD 

       250        260        270        280        290        300 
MAYTPHPCET AAQHSCNADE CGGTYSSSRY AGDCDPDGCD WNPFRMGNKD FYGSGDTVDT 

       310        320        330        340        350        360 
SQKFTVVTQF HGSGSSLTEI SQYYIQGGTK IQQPNSTWPT LTGYNSITDD FCKAQKVEFN 

       370        380        390        400        410        420 
DTDVFSEKGG LAQMGAGMAD GMVLVMSLWD DHYANMLWLD STYPVDADAS SPGKQRGTCA 

       430        440        450 
TTSGVPADVE SSDASATVIY SNIKFGPIGA TY 

« Hide

References

[1]"Induction of a Cryphonectria parasitica cellobiohydrolase I gene is suppressed by hypovirus infection and regulated by a GTP-binding-protein-linked signaling pathway involved in fungal pathogenesis."
Wang P., Nuss D.L.
Proc. Natl. Acad. Sci. U.S.A. 92:11529-11533(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43048 Genomic DNA. Translation: AAB00479.1.

3D structure databases

ProteinModelPortalQ00548.
SMRQ00548. Positions 22-452.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPCBH7A_CRYPA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMALQSETHP.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17643.

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 nameGUX1_CRYPA
AccessionPrimary (citable) accession number: Q00548
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 70 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