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P07982 (GUN2_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHypocrea jecorina (Trichoderma reesei)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.1
Chain22 – 418397Endoglucanase EG-II
PRO_0000007874

Regions

Domain22 – 5736CBM1
Region58 – 9134Linker
Region92 – 418327Catalytic

Sites

Active site2391Proton donor By similarity
Active site3501Nucleophile Ref.3

Amino acid modifications

Modified residue221Pyrrolidone carboxylic acid
Glycosylation1241N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 46 By similarity
Disulfide bond40 ↔ 56 By similarity

Secondary structure

...................................................... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07982 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 26A492D55237A49B

FASTA41844,227
        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 

« Hide

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.
PIRS28372.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QR3X-ray2.05A/B92-418[»]
ProteinModelPortalP07982.
SMRP07982. Positions 23-57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING51453.JGI120312.

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPEGL5C_TRIRE.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2730.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16502.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN2_HYPJE
AccessionPrimary (citable) accession number: P07982
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 16, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries