Reviewed, UniProtKB/Swiss-Prot Q92400 (GUX2_AGABI)

Names and origin

Protein names

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

Gene names

Name:

cel2

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	506 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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. 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 Glycoprotein
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 – 18	18	Potential
	Chain	19 – 506	488	Exoglucanase		PRO_0000007917
Regions
	Domain	470 – 506	37	CBM1
	Region	19 – 450	432	Catalytic
	Region	451 – 473	23	Linker
Sites
	Active site	227	1	Nucleophile By similarity
	Active site	232	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	308	1	N-linked (GlcNAc...) Potential
	Glycosylation	447	1	N-linked (GlcNAc...) Potential
	Disulfide bond	478 ↔ 495		By similarity
	Disulfide bond	489 ↔ 505		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92400-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 0D0390CA4E71BC55	FASTA	506	54,320
	10 20 30 40 50 60 MFPRSILLAL SLTAVALGQQ VGTNMAENHP SLTWQRCTSS GCQNVNGKVT LDANWRWTHR 70 80 90 100 110 120 INDFTNCYTG NEWDTSICPD GVTCAENCAL DGADYAGTYG VTSSGTALTL KFVTESQQKN 130 140 150 160 170 180 IGSRLYLMAD DSNYEIFNLL NKEFTFDVDV SKLPCGLNGA LYFSEMAADG GMSSTNTAGA 190 200 210 220 230 240 KYGTGYCDSQ CPRDIKFIDG EANSEGWEGS PNDVNAGTGN FGACCGEMDI WEANSISSAY 250 260 270 280 290 300 TPHPCREPGL QRCEGNTCSV NDRYATECDP DGCDFNSFRM GDKSFYGPGM TVDTNQPITV 310 320 330 340 350 360 VTQFITDNGS DNGNLQEIRR IYVQNGQVIQ NSNVNIPGID SGNSISAEFC DQAKEAFGDE 370 380 390 400 410 420 RSFQDRGGLS GMGSALDRGM VLVLSIWDDH AVNMLWLDSD YPLDASPSQP GISRGTCSRD 430 440 450 460 470 480 SGKPEDVEAN AGGVQVVYSN IKFGDINSTF NNNGGGGGNP SPTTTRPNSP AQTMWGQCGG 490 500 QGWTGPTACQ SPSTCHVIND FYSQCF

References

[1]

"Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with similarity to fungal cellobiohydrolase I and beta-mannanase, respectively, is regulated by the carbon source." Yague E., Mehak-Zunic M., Morgan L., Wood D.A., Thurston C.F. Microbiology 143:239-244(1997) [PubMed: 9025297] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: D649.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z50094 mRNA. Translation: CAA90422.1.
3D structure databases
SMR	Q92400. Positions 19-451, 472-506.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH7. Glycoside Hydrolase Family 7.
Enzyme and pathway databases
BRENDA	3.2.1.91. 984.
Family and domain databases
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR008985. ConA-like_lec_gl. IPR001722. Glyco_hydro_7. [Graphical view]
Gene3D	G3DSA:2.70.100.10. Glyco_hydro_7. 1 hit.
Pfam	PF00734. CBM_1. 1 hit. PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
ProDom	PD001821. CBD_fun. 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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUX2_AGABI

Accession

Primary (citable) accession number: Q92400

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	February 1, 1997
Last modified:	January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)