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Protein

Endoglucanase EG-II

Gene

egl2

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:3384334). 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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei239Proton donor/acceptor2 Publications1
Active sitei350Nucleophile1 Publication1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16502.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPiEGL5C_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase EG-II (EC:3.2.1.42 Publications)
Short name:
EGII
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:egl2
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000000787422 – 418Endoglucanase EG-IIAdd BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi107 ↔ 113Combined sources1 Publication
Glycosylationi124N-linked (GlcNAc) asparagineBy similarity1
Disulfide bondi183 ↔ 190Combined sources1 Publication
Disulfide bondi323 ↔ 359Combined sources1 Publication
Disulfide bondi364 ↔ 414Combined sources1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi94 – 102Combined sources9
Turni103 – 106Combined sources4
Helixi115 – 117Combined sources3
Beta strandi125 – 129Combined sources5
Helixi134 – 145Combined sources12
Beta strandi149 – 154Combined sources6
Helixi156 – 159Combined sources4
Turni160 – 162Combined sources3
Helixi170 – 185Combined sources16
Beta strandi189 – 194Combined sources6
Turni205 – 208Combined sources4
Helixi212 – 226Combined sources15
Beta strandi232 – 235Combined sources4
Helixi245 – 261Combined sources17
Beta strandi269 – 272Combined sources4
Helixi275 – 277Combined sources3
Turni279 – 285Combined sources7
Helixi287 – 291Combined sources5
Beta strandi304 – 309Combined sources6
Beta strandi316 – 318Combined sources3
Beta strandi320 – 322Combined sources3
Turni328 – 331Combined sources4
Helixi332 – 341Combined sources10
Beta strandi346 – 351Combined sources6
Helixi357 – 371Combined sources15
Turni372 – 376Combined sources5
Beta strandi377 – 386Combined sources10
Beta strandi399 – 403Combined sources5
Helixi409 – 414Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QR3X-ray2.05A/B92-418[»]
ProteinModelPortaliP07982.
SMRiP07982.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 57CBM1PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni58 – 91LinkerCuratedAdd BLAST34
Regioni92 – 418Catalytic1 PublicationAdd BLAST327

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.2 Publications

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IE6V. Eukaryota.
COG2730. LUCA.

Family and domain databases

InterProiView protein in InterPro
IPR035971. CBD_sf.
IPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821. CBD_fun. 1 hit.
SMARTiView protein in SMART
SM00236. fCBD. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiView protein in PROSITE
PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P07982-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKSVAPLLL AASILYGGAV AQQTVWGQCG GIGWSGPTNC APGSACSTLN
60 70 80 90 100
PYYAQCIPGA TTITTSTRPP SGPTTTTRAT STSSSTPPTS SGVRFAGVNI
110 120 130 140 150
AGFDFGCTTD GTCVTSKVYP PLKNFTGSNN YPDGIGQMQH FVNEDGMTIF
160 170 180 190 200
RLPVGWQYLV NNNLGGNLDS TSISKYDQLV QGCLSLGAYC IVDIHNYARW
210 220 230 240 250
NGGIIGQGGP TNAQFTSLWS QLASKYASQS RVWFGIMNEP HDVNINTWAA
260 270 280 290 300
TVQEVVTAIR NAGATSQFIS LPGNDWQSAG AFISDGSAAA LSQVTNPDGS
310 320 330 340 350
TTNLIFDVHK YLDSDNSGTH AECTTNNIDG AFSPLATWLR QNNRQAILTE
360 370 380 390 400
TGGGNVQSCI QDMCQQIQYL NQNSDVYLGY VGWGAGSFDS TYVLTETPTS
410
SGNSWTDTSL VSSCLARK
Length:418
Mass (Da):44,227
Last modified:August 1, 1988 - v1
Checksum:i26A492D55237A49B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19373 Genomic DNA. Translation: AAA34213.1.
PIRiS28372.

Similar proteinsi

Entry informationi

Entry nameiGUN2_HYPJE
AccessioniPrimary (citable) accession number: P07982
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 25, 2017
This is version 112 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-III.1 Publication

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