Reviewed, UniProtKB/Swiss-Prot P07982 (GUN2_TRIRE)

Names and origin

Protein names

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

Gene names

Name:

egl2

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	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	Glycoprotein Pyrrolidone carboxylic acid
Technical term	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	cation binding Inferred from electronic annotation. Source: InterPro 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

Sequences

	Sequence		Length	Mass (Da)
	P07982-1 [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: 3384334] [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: 3356188] [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: 8093602] [Abstract] Cited for: ACTIVE SITE GLU-350.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M19373 Genomic DNA. Translation: AAA34213.1.
PIR	S28372.
3D structure databases
HSSP	HSSP built from PDB template 2CBH based on UniProtKB P00725.
ModBase	Search...
Family and domain databases
InterPro	IPR000254. CBD_fun. IPR001547. Glyco_hydro_5. IPR013781. Glyco_hydro_sub_cat. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00734. CBM_1. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view]
ProDom	PD001821. CBD_fungal. 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. PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN2_TRIRE

Accession

Primary (citable) accession number: P07982

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 25, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)