Reviewed, UniProtKB/Swiss-Prot P07987 (GUX2_TRIRE)

Names and origin

Protein names

Recommended name:
    Exoglucanase 2
    EC=3.2.1.91
Alternative name(s):
    Exoglucanase II
    Exocellobiohydrolase II
      Short name=CBHII
    1,4-beta-cellobiohydrolase

Gene names

Name:

cbh2

Organism

Trichoderma reesei (Hypocrea jecorina)

Taxonomic identifier

51453 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	471 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	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.
Miscellaneous	T.reesei produces two different exocellobiohydrolases. They are unique in that they can hydrolyze crystalline cellulose in the absence of endoglucanases.
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
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure 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: 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 – 24

24

Ref.3

Chain

25 – 471

447

Exoglucanase 2

PRO_0000007911

Regions

Domain

26 – 62

37

CBM1

Region

66 – 106

41

Linker

Region

107 – 471

365

Catalytic

Sites

Active site

199

1

Active site

245

1

Proton donor

Active site

425

1

Nucleophile

Amino acid modifications

Glycosylation

38

1

N-linked (GlcNAc...) Potential

Glycosylation

111

1

O-linked (Man...) Ref.5

Glycosylation

121

1

O-linked (Man...) Ref.5

Glycosylation

130

1

O-linked (Man...) Ref.5

Glycosylation

133

1

O-linked (Man...) Ref.5

Glycosylation

134

1

O-linked (Man...) Ref.5

Glycosylation

139

1

O-linked (Man...) Ref.5

Glycosylation

146

1

O-linked (Man...) Ref.5

Glycosylation

313

1

N-linked (GlcNAc...) Ref.5

Glycosylation

334

1

N-linked (GlcNAc...) Ref.5

Disulfide bond

34 ↔ 51

By similarity

Disulfide bond

45 ↔ 61

By similarity

Disulfide bond

200 ↔ 259

Ref.5

Disulfide bond

392 ↔ 439

Ref.5

Experimental info

Mutagenesis

199

1

D → A: 20% of wild-type activity.

Mutagenesis

245

1

D → A: No measurable activity.

Sequence conflict

359

1

P → R in AAA72922. Ref.2

Sequence conflict

449

1

P → A in AAA72922. Ref.2

Secondary structure

1

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471

Helix Strand Turn

Details...

Turn

116 – 119

4

Helix

126 – 135

10

Helix

137 – 139

3

Helix

142 – 151

10

Beta strand

158 – 160

3

Helix

163 – 165

3

Helix

166 – 181

16

Beta strand

186 – 192

7

Beta strand

202 – 204

3

Helix

211 – 213

3

Helix

215 – 232

18

Turn

233 – 235

3

Beta strand

238 – 242

5

Helix

249 – 252

4

Helix

257 – 276

20

Beta strand

282 – 287

6

Turn

291 – 293

3

Helix

297 – 313

17

Beta strand

320 – 326

7

Helix

340 – 342

3

Helix

350 – 363

14

Beta strand

370 – 374

5

Beta strand

379 – 382

4

Beta strand

392 – 396

5

Beta strand

410 – 416

7

Helix

437 – 440

4

Helix

456 – 464

9

Sequences

	Sequence		Length	Mass (Da)
	P07987-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: C4711BC335B1BD88	FASTA	471	49,653
	10 20 30 40 50 60 MIVGILTTLA TLATLAASVP LEERQACSSV WGQCGGQNWS GPTCCASGST CVYSNDYYSQ 70 80 90 100 110 120 CLPGAASSSS STRAASTTSR VSPTTSRSSS ATPPPGSTTT RVPPVGSGTA TYSGNPFVGV 130 140 150 160 170 180 TPWANAYYAS EVSSLAIPSL TGAMATAAAA VAKVPSFMWL DTLDKTPLME QTLADIRTAN 190 200 210 220 230 240 KNGGNYAGQF VVYDLPDRDC AALASNGEYS IADGGVAKYK NYIDTIRQIV VEYSDIRTLL 250 260 270 280 290 300 VIEPDSLANL VTNLGTPKCA NAQSAYLECI NYAVTQLNLP NVAMYLDAGH AGWLGWPANQ 310 320 330 340 350 360 DPAAQLFANV YKNASSPRAL RGLATNVANY NGWNITSPPS YTQGNAVYNE KLYIHAIGPL 370 380 390 400 410 420 LANHGWSNAF FITDQGRSGK QPTGQQQWGD WCNVIGTGFG IRPSANTGDS LLDSFVWVKP 430 440 450 460 470 GGECDGTSDS SAPRFDSHCA LPDALQPAPQ AGAWFQAYFV QLLTNANPSF L

References

[1]	"Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II." Teeri T.T., Lehtovaara P., Kauppinen S., Salovuori I., Knowles J. Gene 51:43-52(1987) [PubMed: 3596237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VTT-D-80133.
[2]	"Nucleotide sequence and deduced primary structure of cellobiohydrolase II from Trichoderma reesei." Chen C.M., Gritzali M., Stafford D.W. Biotechnology (N.Y.) 5:274-278(1987) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: QM9414 / Rut C-30.
[3]	"The 1,4-beta-glucan cellobiohydrolases of Trichoderma reesei QM 9414." Faegerstam L.G., Pettersson L.G. FEBS Lett. 119:97-100(1980) Cited for: PROTEIN SEQUENCE OF 25-44.
[4]	"Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei." Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K.C., Jones T.A. Science 249:380-386(1990) [PubMed: 2377893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	"The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169." Koivula A., Reinikainen T., Ruohonen L., Valkeajaervi A., Claeyssens M., Teleman O., Kleywegt G.J., Szardenings M., Rouvinen J., Jones T.A., Teeri T.T. Protein Eng. 9:691-699(1996) [PubMed: 8875646] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139; THR-146; ASN-313 AND ASN-334.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M16190 Genomic DNA. Translation: AAA34210.1.
M55080 Genomic DNA. Translation: AAA72922.1.

PIR

A26160.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CB2	X-ray	2.00	A/B	107-471	[»]
1HGW	X-ray	2.10	A/B	107-471	[»]
1HGY	X-ray	2.20	A/B	107-471	[»]
1QJW	X-ray	1.90	A/B	107-471	[»]
1QK0	X-ray	2.10	A/B	109-471	[»]
1QK2	X-ray	2.00	A/B	109-471	[»]
3CBH	X-ray	2.00	A	107-471	[»]

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. 280374.

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

GUX2_TRIRE

Accession

Primary (citable) accession number: P07987

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)