P07982 (GUN2_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase EG-II
Short name=EGLII
EC=3.2.1.4

Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase

Gene names

Name:

egl2

Organism

Hypocrea jecorina (Trichoderma reesei)

Taxonomic identifier

51453 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea › mitosporic Hypocrea › Trichoderma

Protein attributes

Sequence length	418 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.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.
Caution	Was originally called endoglucanase EG-III.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
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: InterPro
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 – 21

21

Ref.1

Chain

22 – 418

397

Endoglucanase EG-II

PRO_0000007874

Regions

Domain

22 – 57

36

CBM1

Region

58 – 91

34

Linker

Region

92 – 418

327

Catalytic

Sites

Active site

239

1

Proton donor By similarity

Active site

350

1

Nucleophile Ref.3

Amino acid modifications

Modified residue

22

1

Pyrrolidone carboxylic acid

Glycosylation

124

1

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 46

By similarity

Disulfide bond

40 ↔ 56

By similarity

Secondary structure

1

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418

Helix Strand Turn

Details...

Beta strand

94 – 102

9

Turn

103 – 106

4

Helix

115 – 117

3

Beta strand

125 – 129

5

Helix

134 – 145

12

Beta strand

149 – 154

6

Helix

156 – 159

4

Turn

160 – 162

3

Helix

170 – 185

16

Beta strand

189 – 194

6

Turn

205 – 208

4

Helix

212 – 226

15

Beta strand

232 – 235

4

Helix

245 – 261

17

Beta strand

269 – 272

4

Helix

275 – 277

3

Turn

279 – 285

7

Helix

287 – 291

5

Beta strand

304 – 309

6

Beta strand

316 – 318

3

Beta strand

320 – 322

3

Turn

328 – 331

4

Helix

332 – 341

10

Beta strand

346 – 351

6

Helix

357 – 371

15

Turn

372 – 376

5

Beta strand

377 – 386

10

Beta strand

399 – 403

5

Helix

409 – 414

6

Sequences

	Sequence		Length	Mass (Da)
	P07982 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 26A492D55237A49B	FASTA	418	44,227
	10 20 30 40 50 60 MNKSVAPLLL AASILYGGAV AQQTVWGQCG GIGWSGPTNC APGSACSTLN PYYAQCIPGA 70 80 90 100 110 120 TTITTSTRPP SGPTTTTRAT STSSSTPPTS SGVRFAGVNI AGFDFGCTTD GTCVTSKVYP 130 140 150 160 170 180 PLKNFTGSNN YPDGIGQMQH FVNEDGMTIF RLPVGWQYLV NNNLGGNLDS TSISKYDQLV 190 200 210 220 230 240 QGCLSLGAYC IVDIHNYARW NGGIIGQGGP TNAQFTSLWS QLASKYASQS RVWFGIMNEP 250 260 270 280 290 300 HDVNINTWAA TVQEVVTAIR NAGATSQFIS LPGNDWQSAG AFISDGSAAA LSQVTNPDGS 310 320 330 340 350 360 TTNLIFDVHK YLDSDNSGTH AECTTNNIDG AFSPLATWLR QNNRQAILTE TGGGNVQSCI 370 380 390 400 410 QDMCQQIQYL NQNSDVYLGY VGWGAGSFDS TYVLTETPTS SGNSWTDTSL VSSCLARK

References

[1]	"EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme." Saloheimo M., Lehtovaara P., Penttilae M., Teeri T.T., Staahlberg J., Johansson G., Pettersson G., Clayssens M., Tomme P., Knowles J.K.C. Gene 63:11-21(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-58, PYROGLUTAMATE FORMATION AT GLN-22. Strain: VTT-D-80133.
[2]	"A binding-site-deficient, catalytically active, core protein of endoglucanase III from the culture filtrate of Trichoderma reesei." Stahlberg J., Johansson G., Pettersson G. Eur. J. Biochem. 173:179-183(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 87-99.
[3]	"Identification of an essential glutamate residue in the active site of endoglucanase III from Trichoderma reesei." Macarron R., van Beeumen J., Henrissat B., de la Mata I., Claeyssens M. FEBS Lett. 316:137-140(1993) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE GLU-350.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19373 Genomic DNA. Translation: AAA34213.1.

PIR

S28372.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QR3	X-ray	2.05	A/B	92-418	[»]

ProteinModelPortal

P07982.

SMR

P07982. Positions 23-57.

ModBase

Search...

Protein-protein interaction databases

STRING

51453.JGI120312.

Protein family/group databases

CAZy

CBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.

mycoCLAP

EGL5C_TRIRE.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG2730.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16502.

Family and domain databases

Gene3D

3.20.20.80. 1 hit.

InterPro

IPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]

ProDom

PD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00236. fCBD. 1 hit.
[Graphical view]

SUPFAM

SSF57180. CBD_fun. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUN2_HYPJE

Accession

Primary (citable) accession number: P07982

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program