Reviewed, UniProtKB/Swiss-Prot Q00548 (GUX1_CRYPA)

Names and origin

Protein names

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

Gene names

Name:

CBH-1

Organism

Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)

Taxonomic identifier

5116 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Diaporthales › Cryphonectriaceae › Cryphonectria-Endothia complex › Cryphonectria

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cellulose 1,4-beta-cellobiosidase activity Inferred from electronic annotation. Source: EC
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 – 452	434	Exoglucanase 1		PRO_0000007920
Sites
	Active site	230	1	Nucleophile By similarity
	Active site	235	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	335	1	N-linked (GlcNAc...) Potential
	Glycosylation	360	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q00548-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5802FD112C2CA864	FASTA	452	48,358
	10 20 30 40 50 60 MFSKFALTGS LLAGAVNAQG VGTQQTETHP QMTWQSCTSP SSCTTNQGEV VIDSNWRWVH 70 80 90 100 110 120 DKDGYVNCYT GNTWNTTLCP DDKTCAANCV LDGADYSSTY GITTSGNALS LQFVTQSSGK 130 140 150 160 170 180 NIGSRTYLME SSTKYHLFDL IGNEFAFDVD LSKLPCGLNG ALYFVTMDAD GGMAKYSTNT 190 200 210 220 230 240 AGAEYGTGYC DSQCPRDLKF INGQGNVEGW TPSTNDANAG VGGLGSCCSE MDVWEANSMD 250 260 270 280 290 300 MAYTPHPCET AAQHSCNADE CGGTYSSSRY AGDCDPDGCD WNPFRMGNKD FYGSGDTVDT 310 320 330 340 350 360 SQKFTVVTQF HGSGSSLTEI SQYYIQGGTK IQQPNSTWPT LTGYNSITDD FCKAQKVEFN 370 380 390 400 410 420 DTDVFSEKGG LAQMGAGMAD GMVLVMSLWD DHYANMLWLD STYPVDADAS SPGKQRGTCA 430 440 450 TTSGVPADVE SSDASATVIY SNIKFGPIGA TY

References

[1]

"Induction of a Cryphonectria parasitica cellobiohydrolase I gene is suppressed by hypovirus infection and regulated by a GTP-binding-protein-linked signaling pathway involved in fungal pathogenesis." Wang P., Nuss D.L. Proc. Natl. Acad. Sci. U.S.A. 92:11529-11533(1995) [PubMed: 8524797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	L43048 Genomic DNA. Translation: AAB00479.1.
3D structure databases
SMR	Q00548. Positions 22-452.
ModBase	Search...
Protein family/group databases
CAZy	GH7. Glycoside Hydrolase Family 7.
Enzyme and pathway databases
BRENDA	3.2.1.91. 274559.
Family and domain databases
InterPro	IPR008985. ConA-like_lec_gl. IPR001722. Glyco_hydro_7. [Graphical view]
Gene3D	G3DSA:2.70.100.10. Glyco_hydro_7. 1 hit.
Pfam	PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
ProtoNet	Search...

Entry information

Entry name

GUX1_CRYPA

Accession

Primary (citable) accession number: Q00548

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)