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P23776

- EXG1_YEAST

UniProt

P23776 - EXG1_YEAST

Protein

Glucan 1,3-beta-glucosidase I/II

Gene

EXG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase.

    Catalytic activityi

    Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei232 – 2321Proton donorBy similarity
    Active sitei334 – 3341NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: SGD

    GO - Biological processi

    1. cellular glucan metabolic process Source: SGD
    2. fungal-type cell wall organization Source: SGD

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciYEAST:YLR300W-MONOMER.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEXG5A_YEAST.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase I/II (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase I/II
    Soluble cell wall protein 6
    Gene namesi
    Name:EXG1
    Synonyms:BGL1, SCW6
    Ordered Locus Names:YLR300W
    ORF Names:L8003.3
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR300w.
    SGDiS000004291. EXG1.

    Subcellular locationi

    Secretedcell wall 1 Publication. Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: SGD
    2. fungal-type cell wall Source: SGD

    Keywords - Cellular componenti

    Cell wall, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 40214 PublicationsPRO_0000007892Add
    BLAST
    Chaini41 – 448408Glucan 1,3-beta-glucosidase I/IIPRO_0000007893Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi165 – 1651N-linked (GlcNAc...)1 Publication
    Glycosylationi325 – 3251N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Glycoprotein

    Proteomic databases

    MaxQBiP23776.
    PaxDbiP23776.
    PeptideAtlasiP23776.

    2D gel databases

    COMPLUYEAST-2DPAGEP23776.

    Miscellaneous databases

    PMAP-CutDBP23776.

    Expressioni

    Gene expression databases

    GenevestigatoriP23776.

    Interactioni

    Protein-protein interaction databases

    BioGridi31564. 57 interactions.
    DIPiDIP-6384N.
    IntActiP23776. 1 interaction.
    MINTiMINT-680007.
    STRINGi4932.YLR300W.

    Structurei

    Secondary structure

    1
    448
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi53 – 575
    Beta strandi61 – 633
    Turni66 – 683
    Helixi70 – 745
    Helixi90 – 978
    Helixi99 – 11315
    Helixi116 – 1249
    Beta strandi129 – 1357
    Helixi136 – 1383
    Helixi152 – 16514
    Beta strandi169 – 1768
    Helixi185 – 1873
    Helixi198 – 21417
    Helixi218 – 2214
    Beta strandi224 – 2296
    Helixi235 – 2373
    Helixi240 – 2467
    Helixi248 – 25710
    Beta strandi265 – 2684
    Helixi276 – 2794
    Helixi283 – 2853
    Beta strandi289 – 2968
    Helixi302 – 3054
    Helixi309 – 32315
    Beta strandi327 – 3359
    Beta strandi339 – 3413
    Turni344 – 3474
    Turni373 – 3764
    Helixi378 – 3803
    Helixi383 – 40018
    Turni401 – 4044
    Beta strandi405 – 4095
    Helixi421 – 4266
    Helixi442 – 4443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H4PX-ray1.75A/B41-448[»]
    ProteinModelPortaliP23776.
    SMRiP23776. Positions 41-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23776.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    GeneTreeiENSGT00390000009809.
    HOGENOMiHOG000114462.
    KOiK01210.
    OMAiHHEYQVF.
    OrthoDBiEOG7JT75H.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23776-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSLKTLLCT LLTVSSVLAT PVPARDPSSI QFVHEENKKR YYDYDHGSLG    50
    EPIRGVNIGG WLLLEPYITP SLFEAFRTND DNDEGIPVDE YHFCQYLGKD 100
    LAKSRLQSHW STFYQEQDFA NIASQGFNLV RIPIGYWAFQ TLDDDPYVSG 150
    LQESYLDQAI GWARNNSLKV WVDLHGAAGS QNGFDNSGLR DSYKFLEDSN 200
    LAVTTNVLNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM DKMKNDYLAP 250
    AYEYLRNNIK SDQVIIIHDA FQPYNYWDDF MTENDGYWGV TIDHHHYQVF 300
    ASDQLERSID EHIKVACEWG TGVLNESHWT VCGEFAAALT DCTKWLNSVG 350
    FGARYDGSWV NGDQTSSYIG SCANNDDIAY WSDERKENTR RYVEAQLDAF 400
    EMRGGWIIWC YKTESSLEWD AQRLMFNGLF PQPLTDRKYP NQCGTISN 448
    Length:448
    Mass (Da):51,311
    Last modified:November 1, 1991 - v1
    Checksum:iF0AD512E410375BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411Y → Q AA sequence (PubMed:9748433)Curated
    Sequence conflicti46 – 461H → G AA sequence (PubMed:9748433)Curated
    Sequence conflicti77 – 771R → H AA sequence (PubMed:2125957)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34341 Genomic DNA. Translation: AAA34599.1.
    U17243 Genomic DNA. Translation: AAB67345.1.
    AY693069 Genomic DNA. Translation: AAT93088.1.
    BK006945 Genomic DNA. Translation: DAA09610.1.
    PIRiJN0118.
    RefSeqiNP_013403.1. NM_001182188.1.

    Genome annotation databases

    EnsemblFungiiYLR300W; YLR300W; YLR300W.
    GeneIDi851007.
    KEGGisce:YLR300W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34341 Genomic DNA. Translation: AAA34599.1 .
    U17243 Genomic DNA. Translation: AAB67345.1 .
    AY693069 Genomic DNA. Translation: AAT93088.1 .
    BK006945 Genomic DNA. Translation: DAA09610.1 .
    PIRi JN0118.
    RefSeqi NP_013403.1. NM_001182188.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H4P X-ray 1.75 A/B 41-448 [» ]
    ProteinModelPortali P23776.
    SMRi P23776. Positions 41-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31564. 57 interactions.
    DIPi DIP-6384N.
    IntActi P23776. 1 interaction.
    MINTi MINT-680007.
    STRINGi 4932.YLR300W.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EXG5A_YEAST.

    2D gel databases

    COMPLUYEAST-2DPAGE P23776.

    Proteomic databases

    MaxQBi P23776.
    PaxDbi P23776.
    PeptideAtlasi P23776.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR300W ; YLR300W ; YLR300W .
    GeneIDi 851007.
    KEGGi sce:YLR300W.

    Organism-specific databases

    CYGDi YLR300w.
    SGDi S000004291. EXG1.

    Phylogenomic databases

    eggNOGi COG2730.
    GeneTreei ENSGT00390000009809.
    HOGENOMi HOG000114462.
    KOi K01210.
    OMAi HHEYQVF.
    OrthoDBi EOG7JT75H.

    Enzyme and pathway databases

    BioCyci YEAST:YLR300W-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P23776.
    NextBioi 967558.
    PMAP-CutDB P23776.

    Gene expression databases

    Genevestigatori P23776.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the exo-1,3-beta-glucanase-encoding gene, EXG1, of the yeast Saccharomyces cerevisiae."
      Vazquez de Aldana C.R., Correa J., San Segundo P., Bueno A., Nebreda A.R., Mendez E., del Rey F.
      Gene 97:173-182(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 41-48.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Two glycosylation patterns for a single protein (exoglucanase) in Saccharomyces cerevisiae."
      Ramirez M., Munoz M.D., Basco R.D., Gimenez-Gallego G., Hernandez L.M., Larriba G.
      FEMS Microbiol. Lett. 59:43-48(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-86.
    6. "Reduced efficiency in the glycosylation of the first sequon of Saccharomyces cerevisiae exoglucanase leads to the synthesis and secretion of a new glycoform of the molecule."
      Basco R.D., Munoz M.D., Hernandez L.M., Vazquez de Aldana C., Larriba G.
      Yeast 9:221-234(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-65.
    7. "New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating."
      Cappellaro C., Mrsa V., Tanner W.
      J. Bacteriol. 180:5030-5037(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-51, SUBCELLULAR LOCATION.
      Strain: ATCC 96099 / S288c / SEY6210.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation."
      Taylor S.C., Ferguson A.D., Bergeron J.J.M., Thomas D.Y.
      Nat. Struct. Mol. Biol. 11:128-134(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 41-448, GLYCOSYLATION AT ASN-165 AND ASN-325.

    Entry informationi

    Entry nameiEXG1_YEAST
    AccessioniPrimary (citable) accession number: P23776
    Secondary accession number(s): D6VYU4, Q9UR92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 4280 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3