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P07981 (GUN1_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 106. 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-1

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:egl1
OrganismHypocrea jecorina (Trichoderma reesei)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length459 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.

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 processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 459437Endoglucanase EG-1
PRO_0000007915

Regions

Domain423 – 45937CBM1
Region23 – 397375Catalytic
Region398 – 42326Linker

Sites

Active site1491 Ref.3
Active site2181Nucleophile
Active site2231Proton donor

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation3941N-linked (GlcNAc...) Potential
Disulfide bond431 ↔ 448 By similarity
Disulfide bond442 ↔ 458 By similarity

Secondary structure

..... 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07981 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: D235A256F808CBB9

FASTA45948,208
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 23-393, PYROGLUTAMATE FORMATION AT GLN-23.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15665 Genomic DNA. Translation: AAA34212.1.
PIRA25928.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG1X-ray3.60A/C24-393[»]
4BMFNMR-A422-459[»]
ProteinModelPortalP07981.
SMRP07981. Positions 23-393, 424-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING51453.JGI122081.

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPEGL7A_TRIRE.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG309529.
OMANSRANAL.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16501.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07981.

Entry information

Entry nameGUN1_HYPJE
AccessionPrimary (citable) accession number: P07981
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 16, 2013
This is version 106 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