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Q00548

- GUX1_CRYPA

UniProt

Q00548 - GUX1_CRYPA

Protein

Exoglucanase 1

Gene

CBH-1

Organism
Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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

    Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei230 – 2301NucleophileBy similarity
    Active sitei235 – 2351Proton donorBy similarity

    GO - Molecular functioni

    1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC

    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-17643.

    Protein family/group databases

    CAZyiGH7. Glycoside Hydrolase Family 7.
    mycoCLAPiCBH7A_CRYPA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoglucanase 1 (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase I
    Beta-glucancellobiohydrolase I
    Exocellobiohydrolase I
    Exoglucanase I
    Gene namesi
    Name:CBH-1
    OrganismiCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
    Taxonomic identifieri5116 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 452434Exoglucanase 1PRO_0000007920Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ00548.
    SMRiQ00548. Positions 22-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OMAiLQSETHP.

    Family and domain databases

    Gene3Di2.70.100.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view]
    PfamiPF00840. Glyco_hydro_7. 1 hit.
    [Graphical view]
    PRINTSiPR00734. GLHYDRLASE7.
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q00548-1 [UniParc]FASTAAdd to Basket

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    MFSKFALTGS LLAGAVNAQG VGTQQTETHP QMTWQSCTSP SSCTTNQGEV    50
    VIDSNWRWVH DKDGYVNCYT GNTWNTTLCP DDKTCAANCV LDGADYSSTY 100
    GITTSGNALS LQFVTQSSGK NIGSRTYLME SSTKYHLFDL IGNEFAFDVD 150
    LSKLPCGLNG ALYFVTMDAD GGMAKYSTNT AGAEYGTGYC DSQCPRDLKF 200
    INGQGNVEGW TPSTNDANAG VGGLGSCCSE MDVWEANSMD MAYTPHPCET 250
    AAQHSCNADE CGGTYSSSRY AGDCDPDGCD WNPFRMGNKD FYGSGDTVDT 300
    SQKFTVVTQF HGSGSSLTEI SQYYIQGGTK IQQPNSTWPT LTGYNSITDD 350
    FCKAQKVEFN DTDVFSEKGG LAQMGAGMAD GMVLVMSLWD DHYANMLWLD 400
    STYPVDADAS SPGKQRGTCA TTSGVPADVE SSDASATVIY SNIKFGPIGA 450
    TY 452
    Length:452
    Mass (Da):48,358
    Last modified:November 1, 1996 - v1
    Checksum:i5802FD112C2CA864
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L43048 Genomic DNA. Translation: AAB00479.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L43048 Genomic DNA. Translation: AAB00479.1 .

    3D structure databases

    ProteinModelPortali Q00548.
    SMRi Q00548. Positions 22-452.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi CBH7A_CRYPA.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OMAi LQSETHP.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17643.

    Family and domain databases

    Gene3Di 2.70.100.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view ]
    Pfami PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00734. GLHYDRLASE7.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Induction of a Cryphonectria parasitica cellobiohydrolase I gene is suppressed by hypovirus infection and regulated by a GTP-binding-protein-linked signaling pathway involved in fungal pathogenesis."
      Wang P., Nuss D.L.
      Proc. Natl. Acad. Sci. U.S.A. 92:11529-11533(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGUX1_CRYPA
    AccessioniPrimary (citable) accession number: Q00548
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3