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P49075 (GUX3_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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 3

EC=3.2.1.91
Alternative name(s):
1,4-beta-cellobiohydrolase 3
Exocellobiohydrolase 3
Gene names
Name:cel3
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Shows enzymatic activity towards crystalline cellulose. At long reaction times. It is also able to degrade carboxymethyl cellulose and barley B-glucan.

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 6 (cellulase B) family.

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 438418Exoglucanase 3
PRO_0000007902

Regions

Domain21 – 5939CBM1
Region60 – 8728Linker
Region88 – 438351Catalytic

Sites

Active site2151Proton donor By similarity
Active site3931Nucleophile By similarity

Amino acid modifications

Disulfide bond28 ↔ 45 By similarity
Disulfide bond39 ↔ 55 By similarity
Disulfide bond170 ↔ 229 By similarity
Disulfide bond360 ↔ 407 By similarity

Natural variations

Natural variant1331V → T.
Natural variant1521R → Q.
Natural variant2441V → I.
Natural variant2481N → D.
Natural variant3981N → S.

Sequences

Sequence LengthMass (Da)Tools
P49075 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 002C973544893794

FASTA43846,210
        10         20         30         40         50         60 
MFKFAALLAL ASLVPGFVQA QSPVWGQCGG NGWTGPTTCA SGSTCVKQND FYSQCLPNNQ 

        70         80         90        100        110        120 
APPSTTTQPG TTPPATTTSG GTGPTSGAGN PYTGKTVWLS PFYADEVAQA AADISNPSLA 

       130        140        150        160        170        180 
TKAASVAKIP TFVWFDTVAK VPDLGGYLAD ARSKNQLVQI VVYDLPDRDC AALASNGEFS 

       190        200        210        220        230        240 
LANDGLNKYK NYVDQIAAQI KQFPDVSVVA VIEPDSLANL VTNLNVQKCA NAQSAYKEGV 

       250        260        270        280        290        300 
IYAVQKLNAV GVTMYIDAGH AGWLGWPANL SPAAQLFAQI YRDAGSPRNL RGIATNVANF 

       310        320        330        340        350        360 
NALRASSPDP ITQGNSNYDE IHYIEALAPM LSNAGFPAHF IVDQGRSGVQ NIRDQWGDWC 

       370        380        390        400        410        420 
NVKGAGFGQR PTTNTGSSLI DAIVWVKPGG ECDGTSDNSS PRFDSHCSLS DAHQPAPEAG 

       430 
TWFQAYFETL VANANPAL 

« Hide

References

[1]"The cel3 gene of Agaricus bisporus codes for a modular cellulase and is transcriptionally regulated by the carbon source."
Chow C.-M., Yague E., Raguz S., Wood D.A., Thurston C.F.
Appl. Environ. Microbiol. 60:2779-2785(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 255-277 AND 331-351.
Strain: D649.
[2]"Correlation of exons with functional domains and folding regions in a cellulase from Agaricus bisporus."
Yague E., Chow C.-M., Challen M.P., Thurston C.F.
Curr. Genet. 30:56-61(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Mycelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L24519 mRNA. Translation: AAA50607.1.
L24520 mRNA. Translation: AAA50608.1.
Z34007 Genomic DNA. Translation: CAA83971.1.
PIRS70602.

3D structure databases

ProteinModelPortalP49075.
SMRP49075. Positions 25-56, 86-438.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPCBH6C_AGABI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMAKCANAQS.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17626.

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 nameGUX3_AGABI
AccessionPrimary (citable) accession number: P49075
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 69 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