Reviewed, UniProtKB/Swiss-Prot Q9P8P3 (GUX1_TRIHA)

Names and origin

Protein names

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

Gene names

Name:

cbh1

Organism

Trichoderma harzianum (Hypocrea lixii)

Taxonomic identifier

5544 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length	505 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.
Subcellular location	Secreted.
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
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 17	17	Potential
	Chain	18 – 505	488	Exoglucanase 1		PRO_0000007925
Regions
	Domain	469 – 505	37	CBM1
	Region	18 – 449	432	Catalytic
	Region	450 – 469	20	Linker
Sites
	Active site	139	1	By similarity
	Active site	225	1	Nucleophile By similarity
	Active site	230	1	Proton donor By similarity
Amino acid modifications
	Modified residue	18	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Glycosylation	126	1	N-linked (GlcNAc...) Potential
	Glycosylation	283	1	N-linked (GlcNAc...) Potential
	Glycosylation	397	1	N-linked (GlcNAc...) Potential
	Disulfide bond	21 ↔ 88		By similarity
	Disulfide bond	36 ↔ 41		By similarity
	Disulfide bond	66 ↔ 87		By similarity
	Disulfide bond	77 ↔ 83		By similarity
	Disulfide bond	151 ↔ 410		By similarity
	Disulfide bond	185 ↔ 223		By similarity
	Disulfide bond	189 ↔ 222		By similarity
	Disulfide bond	243 ↔ 269		By similarity
	Disulfide bond	251 ↔ 256		By similarity
	Disulfide bond	274 ↔ 344		By similarity
	Disulfide bond	477 ↔ 494		By similarity
	Disulfide bond	488 ↔ 504		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9P8P3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 52930722F97D7BF0	FASTA	505	53,216
	10 20 30 40 50 60 MYRKLAVISA FLAAARAQQV CTQQAETHPP LTWQKCTASG CTPQQGSVVL DANWRWTHDT 70 80 90 100 110 120 KSTTNCYDGN TWSSTLCPDD ATCAKNCCLD GANYSGTYGV TTSGDALTLQ FVTASNVGSR 130 140 150 160 170 180 LYLMANDSTY QEFTLSGNEF SFDVDVSQLP CGLNGALYFV SMDADGGQSK YPGNAAGAKY 190 200 210 220 230 240 GTGYCDSQCP RDLKFINGQA NVEGWEPSSN NANTGVGGHG SCCSEMDIWE ANSISEALTP 250 260 270 280 290 300 HPCETVGQTM CSGDSCGGTY SNDRYGGTCD PDGCDWNPYR LGNTSFYGPG SSFALDTTKK 310 320 330 340 350 360 LTVVTQFATD GSISRYYVQN GVKFQQPNAQ VGSYSGNTIN TDYCAAEQTA FGGTSFTDKG 370 380 390 400 410 420 GLAQINKAFQ GGMVLVMSLW DDYAVNMLWL DSTYPTNATA STPGAKRGSC STSSGVPAQV 430 440 450 460 470 480 EAQSPNSKVI YSNIRFGPIG STGGNTGSNP PGTSTTRAPP SSTGSSPTAT QTHYGQCGGT 490 500 GWTGPTRCAS GYTCQVLNPF YSQCL

References

[1]	"Cloning and sequencing of a cellobiohydrolase gene from Trichoderma harzianum FP 108." Guilfoile P.G., Burns R., Gu Z.-Y., Amundson M., Chang F.-H. J. Minn. Acad. Sci. 64:18-22(1999) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FP 108.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF223252 Genomic DNA. Translation: AAF36391.1.
3D structure databases
HSSP	HSSP built from PDB template 6CEL based on UniProtKB P00725.
SMR	Q9P8P3. Positions 18-447.
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. 3745.
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_TRIHA

Accession

Primary (citable) accession number: Q9P8P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)