Reviewed, UniProtKB/Swiss-Prot O59843 (GUX1_ASPAC)

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:

cbhI

Organism

Aspergillus aculeatus

Taxonomic identifier

5053 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	540 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 – 22	22	Potential
	Chain	23 – 540	518	Exoglucanase 1		PRO_0000007918
Regions
	Domain	505 – 540	36	CBM1
	Region	23 – 459	437	Catalytic
	Region	460 – 505	46	Linker
Sites
	Active site	234	1	Nucleophile By similarity
	Active site	239	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	434	1	N-linked (GlcNAc...) Potential
	Glycosylation	458	1	N-linked (GlcNAc...) Potential
	Disulfide bond	513 ↔ 529		By similarity
	Disulfide bond	524 ↔ 539		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O59843-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 002D7FD28DF194D0	FASTA	540	57,099
	10 20 30 40 50 60 MVDSFSIYKT ALLLSMLATS NAQQVGTYTA ETHPSLTWQT CSGSGSCTTT SGSVVIDANW 70 80 90 100 110 120 RWVHEVGGYT NCYSGNTWDS SICSTDTTCA SECALEGATY ESTYGVTTSG SSLRLNFVTT 130 140 150 160 170 180 ASQKNIGSRL YLLADDSTYE TFKLFNREFT FDVDVSNLPC GLNGALYFVS MDADGGVSRF 190 200 210 220 230 240 PTNKAGAKYG TGYCDSQCPR DLKFIDGQAN IEGWEPSSTD VNAGTGNHGS CCPEMDIWEA 250 260 270 280 290 300 NSISSAFTAH PCDSVQQTMC TGDTCGGTYS DTTDRYSGTC DPDGCDFNPY RFGNTNFYGP 310 320 330 340 350 360 GKTVDNSKPF TVVTQFITHD GTDTGTLTEI RRLYVQNGVV IGNGPSTYTA ASGNSITESF 370 380 390 400 410 420 CKAEKTLFGD TNVFETHGGL SAMGDALGDG MVLVLSLWDD HAADMLWLDS DYPTTSCASS 430 440 450 460 470 480 PGVARGTCPT TTGNATYVEA NYPNSYVTYS NIKFGTLNST YSGTSSGGSS SSSTTLTTKA 490 500 510 520 530 540 STSTTSSKTT TTTSKTSTTS SSSTNVAQLY GQCGGQGWTG PTTCASGTCT KQNDYYSQCL

References

[1]	"Cloning, nucleotide sequence, and transcriptional analysis of Aspergillus aculeatus No.F-50 cellobiohydrolase I (cbhI) gene." Takada G., Kawaguchi T., Sumitani J., Arai M. J. Ferment. Bioeng. 85:1-9(1998) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: F-50.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB002821 mRNA. Translation: BAA25183.1.
3D structure databases
HSSP	HSSP built from PDB template 1AZ6 based on UniProtKB P00725.
SMR	O59843. Positions 23-462.
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. 97085.
Family and domain databases
InterPro	IPR000254. CBD_fun. 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_fungal. 1 hit. PD186135. Glyco_hydro_7. 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

GUX1_ASPAC

Accession

Primary (citable) accession number: O59843

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	April 14, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)