Reviewed, UniProtKB/Swiss-Prot P07981 (GUN1_TRIRE)

Names and origin

Protein names

Recommended name:
    Endoglucanase EG-1
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase
    Cellulase

Gene names

Name:

egl1

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	459 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	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
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
Technical term	3D-structure
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	cellulase 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

Chain

23 – 459

437

Endoglucanase EG-1

PRO_0000007915

Regions

Domain

423 – 459

37

CBM1

Region

23 – 397

375

Catalytic

Region

398 – 423

26

Linker

Sites

Active site

149

1

Ref.3

Active site

218

1

Nucleophile

Active site

223

1

Proton donor

Amino acid modifications

Glycosylation

78

1

N-linked (GlcNAc...) Potential

Glycosylation

164

1

N-linked (GlcNAc...) Potential

Glycosylation

204

1

N-linked (GlcNAc...) Potential

Glycosylation

208

1

N-linked (GlcNAc...) Potential

Glycosylation

394

1

N-linked (GlcNAc...) Potential

Disulfide bond

431 ↔ 448

By similarity

Disulfide bond

442 ↔ 458

By similarity

Secondary structure

1

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459

Helix Strand Turn

Details...

Beta strand

27 – 29

3

Beta strand

38 – 42

5

Turn

43 – 45

3

Beta strand

46 – 50

5

Beta strand

53 – 56

4

Helix

58 – 60

3

Beta strand

70 – 73

4

Turn

79 – 81

3

Beta strand

83 – 85

3

Helix

86 – 91

6

Turn

99 – 103

5

Beta strand

104 – 106

3

Beta strand

108 – 115

8

Beta strand

120 – 125

6

Beta strand

130 – 134

5

Beta strand

138 – 140

3

Beta strand

148 – 154

7

Beta strand

163 – 170

8

Turn

174 – 177

4

Helix

185 – 188

4

Beta strand

201 – 203

3

Beta strand

218 – 224

7

Beta strand

231 – 234

4

Turn

250 – 254

5

Beta strand

258 – 260

3

Beta strand

263 – 265

3

Beta strand

271 – 279

9

Beta strand

288 – 297

10

Beta strand

310 – 312

3

Helix

317 – 321

5

Turn

322 – 324

3

Helix

325 – 333

9

Beta strand

335 – 343

9

Turn

345 – 349

5

Helix

350 – 353

4

Helix

355 – 357

3

Turn

362 – 365

4

Helix

367 – 373

7

Beta strand

378 – 388

11

Turn

389 – 391

3

Sequences

	Sequence		Length	Mass (Da)
	P07981-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: D235A256F808CBB9	FASTA	459	48,208
	10 20 30 40 50 60 MAPSVTLPLT TAILAIARLV AAQQPGTSTP EVHPKLTTYK CTKSGGCVAQ DTSVVLDWNY 70 80 90 100 110 120 RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCFIEGVDYA ASGVTTSGSS LTMNQYMPSS 130 140 150 160 170 180 SGGYSSVSPR LYLLDSDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ 190 200 210 220 230 240 YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS HQGFCCNEMD ILEGNSRANA LTPHSCTATA 250 260 270 280 290 300 CDSAGCGFNP YGSGYKSYYG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYQQNGV 310 320 330 340 350 360 DIPSAQPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGNAGPC 370 380 390 400 410 420 SSTEGNPSNI LANNPNTHVV FSNIRWGDIG STTNSTAPPP PPASSTTFST TRRSSTTSSS 430 440 450 PSCTQTHWGQ CGGIGYSGCK TCTSGTTCQY SNDYYSQCL

References

[1]	"Homology between cellulase genes of Trichoderma reesei: complete nucleotide sequence of the endoglucanase I gene." Penttilae M., Lehtovaara P., Nevalainen H., Bhikhabhai R., Knowles J.K.C. Gene 45:253-263(1986) [PubMed: 2948877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VTT-D-80133.
[2]	"Cloning, characterization, and expression in Saccharomyces cerevisiae of endoglucanase I from Trichoderma reesei." van Arsdell J.N., Kwok S., Schweickart V.L., Ladner M.B., Gelfand D.H., Innis M.A. Biotechnology (N.Y.) 5:60-64(1987) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: L27.
[3]	"Identification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei." Tomme P., Clayssens M. FEBS Lett. 243:239-243(1989) Cited for: ACTIVE SITE GLU-149.
[4]	"The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6-A resolution, and a comparison with related enzymes." Kleywegt G.J., Zou J.-Y., Divne C., Davies G.J., Sinning I., Staehlberg J., Reinikainen T., Srisodsuk M., Teeri T.T., Jones T.A. J. Mol. Biol. 272:383-397(1997) [PubMed: 9325098] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 23-393.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15665 Genomic DNA. Translation: AAA34212.1.

PIR

A25928.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EG1	X-ray	3.60	A/C	24-393	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.

Enzyme and pathway databases

BRENDA

3.2.1.4. 280374.

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

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

GUN1_TRIRE

Accession

Primary (citable) accession number: P07981

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)