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Q06886 (GUX1_PENJA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 77. 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
Exocellobiohydrolase I
Exoglucanase I
Gene names
Name:cbh1
OrganismPenicillium janthinellum (Penicillium vitale)
Taxonomic identifier5079 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

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
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 – 1818 Potential
Chain19 – 537519Exoglucanase 1
PRO_0000007923

Regions

Domain501 – 53737CBM1
Region19 – 453435Catalytic
Region454 – 47724Linker

Sites

Active site2351Nucleophile By similarity
Active site2401Proton donor By similarity

Amino acid modifications

Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Disulfide bond509 ↔ 526 By similarity
Disulfide bond520 ↔ 536 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06886 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A6B9C6EB73F17FE4

FASTA53756,845
        10         20         30         40         50         60 
MKGSISYQIY KGALLLSALL NSVSAQQVGT LTAETHPALT WSKCTAGXCS QVSGSVVIDA 

        70         80         90        100        110        120 
NWPXVHSTSG STNCYTGNTW DATLCPDDVT CAANCAVDGA RRQHLRVTTS GNSLRINFVT 

       130        140        150        160        170        180 
TASQKNIGSR LYLLENDTTY QKFNLLNQEF TFDVDVSNLP CGLNGALYFV DMDADGGMAK 

       190        200        210        220        230        240 
YPTNKAGAKY GTGYCDSQCP RDLKFINGQA NVDGWTPSKN DVNSGIGNHG SCCAEMDIWE 

       250        260        270        280        290        300 
ANSISNAVTP HPCDTPSQTM CTGQRCGGTY STDRYGGTCD PDGCDFNPYR MGVTNFYGPG 

       310        320        330        340        350        360 
ETIDTKSPFT VVTQFLTNDG TSTGTLSEIK RFYVQGGKVI GNPQSTIVGV SGNSITDSWC 

       370        380        390        400        410        420 
NAQKSAFGDT NEFSKHGGMA GMGAGLADGM VLVMSLWDDH ASDMLWLDST YPTNATSTTP 

       430        440        450        460        470        480 
GAKRGTCDIS RRPNTVESTY PNAYVIYSNI KTGPLNSTFT GGTTSSSSTT TTTSKSTSTS 

       490        500        510        520        530 
SSSKTTTTVT TTTTSSGSSG TGARDWAQCG GNGWTGPTTC VSPYTCTKQN DWYSQCL 

« Hide

References

[1]"Cloning, sequencing, and heterologous expression of a cellulase-encoding cDNA (cbh1) from Penicillium janthinellum."
Koch A., Weigel C.T.O., Schulz G.
Gene 124:57-65(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C41.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59054 mRNA. Translation: CAA41780.1.
PIRJU0150.

3D structure databases

ProteinModelPortalQ06886.
SMRQ06886. Positions 503-537.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPCBH7A_PENJA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameGUX1_PENJA
AccessionPrimary (citable) accession number: Q06886
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 13, 2013
This is version 77 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