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P07982

- GUN2_HYPJE

UniProt

P07982 - GUN2_HYPJE

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Protein

Endoglucanase EG-II

Gene

egl2

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - Annotation score: 5 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 sitei239 – 2391Proton donorBy similarity
Active sitei350 – 3501Nucleophile1 Publication

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-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:3.2.1.4)
Short name:
EGLII
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:egl2
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 418397Endoglucanase EG-IIPRO_0000007874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Pyrrolidone carboxylic acid1 Publication
Disulfide bondi29 ↔ 46By similarity
Disulfide bondi40 ↔ 56By similarity
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI120312.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi94 – 1029
Turni103 – 1064
Helixi115 – 1173
Beta strandi125 – 1295
Helixi134 – 14512
Beta strandi149 – 1546
Helixi156 – 1594
Turni160 – 1623
Helixi170 – 18516
Beta strandi189 – 1946
Turni205 – 2084
Helixi212 – 22615
Beta strandi232 – 2354
Helixi245 – 26117
Beta strandi269 – 2724
Helixi275 – 2773
Turni279 – 2857
Helixi287 – 2915
Beta strandi304 – 3096
Beta strandi316 – 3183
Beta strandi320 – 3223
Turni328 – 3314
Helixi332 – 34110
Beta strandi346 – 3516
Helixi357 – 37115
Turni372 – 3765
Beta strandi377 – 38610
Beta strandi399 – 4035
Helixi409 – 4146

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QR3X-ray2.05A/B92-418[»]
ProteinModelPortaliP07982.
SMRiP07982. Positions 23-57.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 5736CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 9134LinkerAdd
BLAST
Regioni92 – 418327CatalyticAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07982 [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:
EMBL
GenBank
DDBJ
Links Updated
M19373 Genomic DNA. Translation: AAA34213.1.
PIRiS28372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19373 Genomic DNA. Translation: AAA34213.1 .
PIRi S28372.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QR3 X-ray 2.05 A/B 92-418 [» ]
ProteinModelPortali P07982.
SMRi P07982. Positions 23-57.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 51453.JGI120312.

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPi EGL5C_TRIRE.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2730.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16502.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGUN2_HYPJE
AccessioniPrimary (citable) accession number: P07982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 1, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Was originally called endoglucanase EG-III.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

External Data

Dasty 3