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Q92400

- GUX2_AGABI

UniProt

Q92400 - GUX2_AGABI

Protein

Exoglucanase

Gene

cel2

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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 sitei227 – 2271NucleophileBy similarity
    Active sitei232 – 2321Proton 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 (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Beta-glucancellobiohydrolase
    Exocellobiohydrolase
    Gene namesi
    Name:cel2
    OrganismiAgaricus bisporus (White button mushroom)
    Taxonomic identifieri5341 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 506488ExoglucanasePRO_0000007917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi478 ↔ 495By similarity
    Disulfide bondi489 ↔ 505By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ92400.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92400.
    SMRiQ92400. Positions 19-451, 472-506.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini470 – 50637CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 450432CatalyticAdd
    BLAST
    Regioni451 – 47323LinkerAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OMAiRGTCSRD.

    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.

    Q92400-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFPRSILLAL SLTAVALGQQ VGTNMAENHP SLTWQRCTSS GCQNVNGKVT    50
    LDANWRWTHR INDFTNCYTG NEWDTSICPD GVTCAENCAL DGADYAGTYG 100
    VTSSGTALTL KFVTESQQKN IGSRLYLMAD DSNYEIFNLL NKEFTFDVDV 150
    SKLPCGLNGA LYFSEMAADG GMSSTNTAGA KYGTGYCDSQ CPRDIKFIDG 200
    EANSEGWEGS PNDVNAGTGN FGACCGEMDI WEANSISSAY TPHPCREPGL 250
    QRCEGNTCSV NDRYATECDP DGCDFNSFRM GDKSFYGPGM TVDTNQPITV 300
    VTQFITDNGS DNGNLQEIRR IYVQNGQVIQ NSNVNIPGID SGNSISAEFC 350
    DQAKEAFGDE RSFQDRGGLS GMGSALDRGM VLVLSIWDDH AVNMLWLDSD 400
    YPLDASPSQP GISRGTCSRD SGKPEDVEAN AGGVQVVYSN IKFGDINSTF 450
    NNNGGGGGNP SPTTTRPNSP AQTMWGQCGG QGWTGPTACQ SPSTCHVIND 500
    FYSQCF 506
    Length:506
    Mass (Da):54,320
    Last modified:February 1, 1997 - v1
    Checksum:i0D0390CA4E71BC55
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50094 mRNA. Translation: CAA90422.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50094 mRNA. Translation: CAA90422.1 .

    3D structure databases

    ProteinModelPortali Q92400.
    SMRi Q92400. Positions 19-451, 472-506.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Proteomic databases

    PRIDEi Q92400.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OMAi RGTCSRD.

    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. "Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with similarity to fungal cellobiohydrolase I and beta-mannanase, respectively, is regulated by the carbon source."
      Yague E., Mehak-Zunic M., Morgan L., Wood D.A., Thurston C.F.
      Microbiology 143:239-244(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: D649.

    Entry informationi

    Entry nameiGUX2_AGABI
    AccessioniPrimary (citable) accession number: Q92400
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 74 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