Reviewed, UniProtKB/Swiss-Prot P49075 (GUX3_AGABI)

Names and origin

Protein names

Recommended name:
    Exoglucanase 3
    EC=3.2.1.91
Alternative name(s):
    Exocellobiohydrolase 3
    1,4-beta-cellobiohydrolase 3

Gene names

Name:

cel3

Organism

Agaricus bisporus (Common mushroom)

Taxonomic identifier

5341 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	cellulose 1,4-beta-cellobiosidase activity Inferred from electronic annotation. Source: EC cellulose binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 438	418	Exoglucanase 3		PRO_0000007902
Regions
	Domain	21 – 59	39	CBM1
	Region	60 – 87	28	Linker
	Region	88 – 438	351	Catalytic
Sites
	Active site	215	1	Proton donor By similarity
	Active site	393	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	28 ↔ 45		By similarity
	Disulfide bond	39 ↔ 55		By similarity
	Disulfide bond	170 ↔ 229		By similarity
	Disulfide bond	360 ↔ 407		By similarity
Natural variations
	Natural variant	133	1	V → T
	Natural variant	152	1	R → Q
	Natural variant	244	1	V → I
	Natural variant	248	1	N → D
	Natural variant	398	1	N → S

Sequences

	Sequence		Length	Mass (Da)
	P49075-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 002C973544893794	FASTA	438	46,210
	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

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: 8085821] [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: 8662210] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Mycelium.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L24519 mRNA. Translation: AAA50607.1. L24520 mRNA. Translation: AAA50608.1. Z34007 Genomic DNA. Translation: CAA83971.1.
PIR	S70602.
3D structure databases
HSSP	HSSP built from PDB template 1AZ6 based on UniProtKB P00725.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH6. Glycoside Hydrolase Family 6.
Enzyme and pathway databases
BRENDA	3.2.1.91. 984.
Family and domain databases
InterPro	IPR016288. Beta_cellobiohydrolase. IPR000254. CBD_fun. IPR001524. Glyco_hydro_6_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.40. Glyco_hydro_6. 1 hit.
Pfam	PF00734. CBM_1. 1 hit. PF01341. Glyco_hydro_6. 1 hit. [Graphical view]
PIRSF	PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTS	PR00733. GLHYDRLASE6.
ProDom	PD001821. CBD_fungal. 1 hit. PD003733. Glyco_hydro_6. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
PROSITE	PS00562. 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]
ProtoNet	Search...

Entry information

Entry name

GUX3_AGABI

Accession

Primary (citable) accession number: P49075

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)