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Protein

Endoglucanase EG-1

Gene

egl1

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei149 – 14911 Publication
Active sitei218 – 2181Nucleophile
Active sitei223 – 2231Proton donor

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16501.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiEGL7A_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase EG-1 (EC:3.2.1.4)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:egl1
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 459437Endoglucanase EG-1PRO_0000007915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi394 – 3941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi431 ↔ 448By similarity
Disulfide bondi442 ↔ 458By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI122081.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi448 – 4547Combined sources
Beta strandi456 – 4583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG1X-ray3.60A/C24-393[»]
4BMFNMR-A422-459[»]
ProteinModelPortaliP07981.
SMRiP07981. Positions 23-393, 424-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07981.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini423 – 45937CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 397375CatalyticAdd
BLAST
Regioni398 – 42326LinkerAdd
BLAST

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG309529.
OMAiNSRANAL.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07981-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPSVTLPLT TAILAIARLV AAQQPGTSTP EVHPKLTTYK CTKSGGCVAQ
60 70 80 90 100
DTSVVLDWNY RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCFIEGVDYA
110 120 130 140 150
ASGVTTSGSS LTMNQYMPSS SGGYSSVSPR LYLLDSDGEY VMLKLNGQEL
160 170 180 190 200
SFDVDLSALP CGENGSLYLS QMDENGGANQ YNTAGANYGS GYCDAQCPVQ
210 220 230 240 250
TWRNGTLNTS HQGFCCNEMD ILEGNSRANA LTPHSCTATA CDSAGCGFNP
260 270 280 290 300
YGSGYKSYYG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYQQNGV
310 320 330 340 350
DIPSAQPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN
360 370 380 390 400
WLDSGNAGPC SSTEGNPSNI LANNPNTHVV FSNIRWGDIG STTNSTAPPP
410 420 430 440 450
PPASSTTFST TRRSSTTSSS PSCTQTHWGQ CGGIGYSGCK TCTSGTTCQY

SNDYYSQCL
Length:459
Mass (Da):48,208
Last modified:August 1, 1988 - v1
Checksum:iD235A256F808CBB9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15665 Genomic DNA. Translation: AAA34212.1.
PIRiA25928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15665 Genomic DNA. Translation: AAA34212.1.
PIRiA25928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG1X-ray3.60A/C24-393[»]
4BMFNMR-A422-459[»]
ProteinModelPortaliP07981.
SMRiP07981. Positions 23-393, 424-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI122081.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiEGL7A_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG309529.
OMAiNSRANAL.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16501.

Miscellaneous databases

EvolutionaryTraceiP07981.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiGUN1_HYPJE
AccessioniPrimary (citable) accession number: P07981
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 7, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.