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P19355

- GUX1_HYPRU

UniProt

P19355 - GUX1_HYPRU

Protein

Exoglucanase 1

Gene

cbh1

Organism
Hypocrea rufa (Trichoderma viride)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      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 sitei229 – 2291NucleophileBy similarity
    Active sitei234 – 2341Proton donorBy similarity

    GO - Molecular functioni

    1. cellulose 1,4-beta-cellobiosidase 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

    Protein family/group databases

    CAZyiCBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoglucanase 1 (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Exocellobiohydrolase
    Exoglucanase I
    Gene namesi
    Name:cbh1
    OrganismiHypocrea rufa (Trichoderma viride)
    Taxonomic identifieri5547 [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 – 1717Add
    BLAST
    Chaini18 – 514497Exoglucanase 1PRO_0000007928Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 89By similarity
    Disulfide bondi36 ↔ 42By similarity
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi67 ↔ 88By similarity
    Disulfide bondi78 ↔ 84By similarity
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi155 ↔ 414By similarity
    Disulfide bondi189 ↔ 227By similarity
    Disulfide bondi193 ↔ 226By similarity
    Disulfide bondi247 ↔ 273By similarity
    Disulfide bondi255 ↔ 260By similarity
    Disulfide bondi278 ↔ 348By similarity
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi486 ↔ 503By similarity
    Disulfide bondi497 ↔ 513By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP19355.
    SMRiP19355. Positions 18-451, 479-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini478 – 51437CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 453436CatalyticAdd
    BLAST
    Regioni454 – 47825LinkerAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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.
    ProDomiPD001821. CBD_fun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    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.

    P19355-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYQKLALISA FLATARAQSA CTLQAETHPP LTWQKCSSGG TCTQQTGSVV    50
    IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG 100
    VTTSADSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV 150
    SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI 200
    NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV 250
    GQEICDGDSC GGTYSGDRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD 300
    TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGDYSG NSLDDDYCAA 350
    EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT 400
    NETSSTPGAV RGSCSTSSGV PAQLESNSPN AKVVYSNIKF GPIGSTGNSS 450
    GGNPPGGNPP GTTTTRRPAT STGSSPGPTQ THYGQCGGIG YSGPTVCASG 500
    STCQVLNPYY SQCL 514
    Length:514
    Mass (Da):54,002
    Last modified:July 19, 2004 - v2
    Checksum:iC5B1FB734C9CDAF5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731S → T in CAA37878. (PubMed:2216737)Curated
    Sequence conflicti256 – 2561D → E in CAA37878. (PubMed:2216737)Curated
    Sequence conflicti401 – 4011N → D in CAA37878. (PubMed:2216737)Curated
    Sequence conflicti414 – 4141C → S in CAA37878. (PubMed:2216737)Curated
    Sequence conflicti449 – 4491S → P in CAA37878. (PubMed:2216737)Curated
    Sequence conflicti462 – 4621Missing(PubMed:2216737)Curated
    Sequence conflicti466 – 4661R → P(PubMed:2216737)Curated
    Sequence conflicti492 – 4921S → I in CAA37878. (PubMed:2216737)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53931 Genomic DNA. Translation: CAA37878.1.
    AB021656 Genomic DNA. Translation: BAA36215.1.
    PIRiS11439.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53931 Genomic DNA. Translation: CAA37878.1 .
    AB021656 Genomic DNA. Translation: BAA36215.1 .
    PIRi S11439.

    3D structure databases

    ProteinModelPortali P19355.
    SMRi P19355. Positions 18-451, 479-514.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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.
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    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. "Nucleotide sequence of the cellobiohydrolase gene from Trichoderma viride."
      Cheng C., Tsukagoshi N., Udaka S.
      Nucleic Acids Res. 18:5559-5559(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Watanabe M.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: MC300-1.

    Entry informationi

    Entry nameiGUX1_HYPRU
    AccessioniPrimary (citable) accession number: P19355
    Secondary accession number(s): O93832
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 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