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P07982

- GUN2_HYPJE

UniProt

P07982 - GUN2_HYPJE

Protein

Endoglucanase EG-II

Gene

egl2

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    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

    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

    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.

    P07982-1 [UniParc]FASTAAdd to Basket

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    MNKSVAPLLL AASILYGGAV AQQTVWGQCG GIGWSGPTNC APGSACSTLN    50
    PYYAQCIPGA TTITTSTRPP SGPTTTTRAT STSSSTPPTS SGVRFAGVNI 100
    AGFDFGCTTD GTCVTSKVYP PLKNFTGSNN YPDGIGQMQH FVNEDGMTIF 150
    RLPVGWQYLV NNNLGGNLDS TSISKYDQLV QGCLSLGAYC IVDIHNYARW 200
    NGGIIGQGGP TNAQFTSLWS QLASKYASQS RVWFGIMNEP HDVNINTWAA 250
    TVQEVVTAIR NAGATSQFIS LPGNDWQSAG AFISDGSAAA LSQVTNPDGS 300
    TTNLIFDVHK YLDSDNSGTH AECTTNNIDG AFSPLATWLR QNNRQAILTE 350
    TGGGNVQSCI QDMCQQIQYL NQNSDVYLGY VGWGAGSFDS TYVLTETPTS 400
    SGNSWTDTSL VSSCLARK 418
    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