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Protein

Endoglucanase EG-1

Gene

egl1

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

Functioni

Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose (PubMed:2948877). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates new chain ends for exocellobiohydrolases (CBHs). The CBH release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).Curated1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei218Nucleophile1 Publication1
Active sitei223Proton donor/acceptor1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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:3.2.1.41 Publication)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:egl1
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000000791523 – 459Endoglucanase EG-1Add BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Pyrrolidone carboxylic acid2 Publications1
Disulfide bondi41 ↔ 47Combined sources1 Publication
Disulfide bondi71 ↔ 92Combined sources1 Publication
Glycosylationi78N-linked (GlcNAc) asparagineBy similarity1 Publication1
Disulfide bondi82 ↔ 88Combined sources1 Publication
Disulfide bondi161 ↔ 360Combined sources1 Publication
Disulfide bondi193 ↔ 216Combined sources1 Publication
Disulfide bondi197 ↔ 215Combined sources1 Publication
Glycosylationi204N-linked (GlcNAc...) (high mannose) asparagineBy similarity1 Publication1
Disulfide bondi236 ↔ 241Combined sources1 Publication
Disulfide bondi246 ↔ 315Combined sources1 Publication
Glycosylationi394N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi423 ↔ 439Combined sources1 Publication
Disulfide bondi431 ↔ 448Combined sources1 Publication
Disulfide bondi442 ↔ 458Combined sources1 Publication

Post-translational modificationi

Asn-204 contains mainly a high-mannose-type glycan (Hex7-9GlcNAc2), with a small fraction (8%) bearing a single GlcNAc at this site.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei164Not glycosylatedBy similarity1
Sitei208Not glycosylatedBy similarity1
Sitei281Not glycosylatedBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi448 – 454Combined sources7
Beta strandi456 – 458Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP07981.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini423 – 459CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 397Catalytic1 PublicationAdd BLAST375
Regioni398 – 423LinkerCuratedAdd BLAST26

Domaini

The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IUY5. Eukaryota.
ENOG410YC82. LUCA.
OMAiSGYCDAQ.

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
Gene3Di2.70.100.10. 1 hit.
InterProiView protein in InterPro
IPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
PfamiView protein in Pfam
PF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
PRINTSiPR00734. GLHYDRLASE7.
SMARTiView protein in SMART
SM00236. fCBD. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiView protein in PROSITE
PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiGUN1_HYPJE
AccessioniPrimary (citable) accession number: P07981
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: August 30, 2017
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Was originally called endoglucanase EG-II.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

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