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P62695

- GUX1_TRIKO

UniProt

P62695 - GUX1_TRIKO

Protein

Exoglucanase 1

Gene

cbh1

Organism
Trichoderma koningii (Hypocrea koningii)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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 sitei143 – 1431By similarity
    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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17641.

    Protein family/group databases

    CAZyiCBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPiCBH7A_TRIKO.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoglucanase 1 (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Exocellobiohydrolase I
    Short name:
    CBHI
    Exoglucanase I
    Gene namesi
    Name:cbh1
    OrganismiTrichoderma koningii (Hypocrea koningii)
    Taxonomic identifieri97093 [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 – 1717By similarityAdd
    BLAST
    Chaini18 – 513496Exoglucanase 1PRO_0000007926Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Pyrrolidone carboxylic acidBy similarity
    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
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi485 ↔ 502By similarity
    Disulfide bondi496 ↔ 512By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Structurei

    3D structure databases

    ProteinModelPortaliP62695.
    SMRiP62695. Positions 18-451, 478-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini477 – 51337CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 453436CatalyticAdd
    BLAST
    Regioni454 – 47724LinkerAdd
    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.

    P62695-1 [UniParc]FASTAAdd to Basket

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    MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV    50
    IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG 100
    VTTSGNSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV 150
    SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI 200
    NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV 250
    GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD 300
    TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA 350
    EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT 400
    NETSSTPGAV RGSCSTSSGV PAQVESQSPN AKVTFSNIKF GPIGSTGNPS 450
    GGNPPGGNRG TTTTRRPATT TGSSPGPTQS HYGQCGGIGY SGPTVCASGT 500
    TCQVLNPYYS QCL 513
    Length:513
    Mass (Da):54,073
    Last modified:July 21, 1986 - v1
    Checksum:i9F5C0A8A854F2C12
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69976 Genomic DNA. Translation: CAA49596.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69976 Genomic DNA. Translation: CAA49596.1 .

    3D structure databases

    ProteinModelPortali P62695.
    SMRi P62695. Positions 18-451, 478-513.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi CBH7A_TRIKO.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17641.

    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. "Molecular cloning and sequence analysis of the cellobiohydrolase I gene from Trichoderma koningii G-39."
      Wey T.T., Hseu T.H., Huang L.
      Curr. Microbiol. 28:31-39(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: G-39.

    Entry informationi

    Entry nameiGUX1_TRIKO
    AccessioniPrimary (citable) accession number: P62695
    Secondary accession number(s): P00725
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 49 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