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P07981

- GUN1_HYPJE

UniProt

P07981 - GUN1_HYPJE

Protein

Endoglucanase EG-1

Gene

egl1

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (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 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

    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

    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 – 4547
    Beta strandi456 – 4583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    IPR008985. ConA-like_lec_gl_sf.
    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

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    MAPSVTLPLT TAILAIARLV AAQQPGTSTP EVHPKLTTYK CTKSGGCVAQ    50
    DTSVVLDWNY RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCFIEGVDYA 100
    ASGVTTSGSS LTMNQYMPSS SGGYSSVSPR LYLLDSDGEY VMLKLNGQEL 150
    SFDVDLSALP CGENGSLYLS QMDENGGANQ YNTAGANYGS GYCDAQCPVQ 200
    TWRNGTLNTS HQGFCCNEMD ILEGNSRANA LTPHSCTATA CDSAGCGFNP 250
    YGSGYKSYYG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYQQNGV 300
    DIPSAQPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN 350
    WLDSGNAGPC SSTEGNPSNI LANNPNTHVV FSNIRWGDIG STTNSTAPPP 400
    PPASSTTFST TRRSSTTSSS PSCTQTHWGQ CGGIGYSGCK TCTSGTTCQY 450
    SNDYYSQCL 459
    Length:459
    Mass (Da):48,208
    Last modified:August 1, 1988 - v1
    Checksum:iD235A256F808CBB9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15665 Genomic DNA. Translation: AAA34212.1.
    PIRiA25928.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15665 Genomic DNA. Translation: AAA34212.1 .
    PIRi A25928.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EG1 X-ray 3.60 A/C 24-393 [» ]
    4BMF NMR - A 422-459 [» ]
    ProteinModelPortali P07981.
    SMRi P07981. Positions 23-393, 424-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 51453.JGI122081.

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi EGL7A_TRIRE.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG309529.
    OMAi NSRANAL.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16501.

    Miscellaneous databases

    EvolutionaryTracei P07981.

    Family and domain databases

    Gene3Di 2.70.100.10. 1 hit.
    InterProi IPR000254. Cellulose-bd_dom_fun.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00734. GLHYDRLASE7.
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 107 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