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Protein

Exoglucanase 3

Gene

cel3

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei215 – 2151Proton donorPROSITE-ProRule annotation
Active sitei393 – 3931NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17626.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPiCBH6C_AGABI.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 3 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase 3
Exocellobiohydrolase 3
Gene namesi
Name:cel3
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 438418Exoglucanase 3PRO_0000007902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 45By similarity
Disulfide bondi39 ↔ 55By similarity
Disulfide bondi170 ↔ 229By similarity
Disulfide bondi360 ↔ 407By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP49075.
SMRiP49075. Positions 25-56, 86-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 5939CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 8728LinkerAdd
BLAST
Regioni88 – 438351CatalyticAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

OMAiGWPANIQ.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKFAALLAL ASLVPGFVQA QSPVWGQCGG NGWTGPTTCA SGSTCVKQND
60 70 80 90 100
FYSQCLPNNQ APPSTTTQPG TTPPATTTSG GTGPTSGAGN PYTGKTVWLS
110 120 130 140 150
PFYADEVAQA AADISNPSLA TKAASVAKIP TFVWFDTVAK VPDLGGYLAD
160 170 180 190 200
ARSKNQLVQI VVYDLPDRDC AALASNGEFS LANDGLNKYK NYVDQIAAQI
210 220 230 240 250
KQFPDVSVVA VIEPDSLANL VTNLNVQKCA NAQSAYKEGV IYAVQKLNAV
260 270 280 290 300
GVTMYIDAGH AGWLGWPANL SPAAQLFAQI YRDAGSPRNL RGIATNVANF
310 320 330 340 350
NALRASSPDP ITQGNSNYDE IHYIEALAPM LSNAGFPAHF IVDQGRSGVQ
360 370 380 390 400
NIRDQWGDWC NVKGAGFGQR PTTNTGSSLI DAIVWVKPGG ECDGTSDNSS
410 420 430
PRFDSHCSLS DAHQPAPEAG TWFQAYFETL VANANPAL
Length:438
Mass (Da):46,210
Last modified:February 1, 1996 - v1
Checksum:i002C973544893794
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331V → T.
Natural varianti152 – 1521R → Q.
Natural varianti244 – 2441V → I.
Natural varianti248 – 2481N → D.
Natural varianti398 – 3981N → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24519 mRNA. Translation: AAA50607.1.
L24520 mRNA. Translation: AAA50608.1.
Z34007 Genomic DNA. Translation: CAA83971.1.
PIRiS70602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24519 mRNA. Translation: AAA50607.1.
L24520 mRNA. Translation: AAA50608.1.
Z34007 Genomic DNA. Translation: CAA83971.1.
PIRiS70602.

3D structure databases

ProteinModelPortaliP49075.
SMRiP49075. Positions 25-56, 86-438.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPiCBH6C_AGABI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OMAiGWPANIQ.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17626.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. 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]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiGUX3_AGABI
AccessioniPrimary (citable) accession number: P49075
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.