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P23776

- EXG1_YEAST

UniProt

P23776 - EXG1_YEAST

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP23776.
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

        10         20         30         40         50
MLSLKTLLCT LLTVSSVLAT PVPARDPSSI QFVHEENKKR YYDYDHGSLG
60 70 80 90 100
EPIRGVNIGG WLLLEPYITP SLFEAFRTND DNDEGIPVDE YHFCQYLGKD
110 120 130 140 150
LAKSRLQSHW STFYQEQDFA NIASQGFNLV RIPIGYWAFQ TLDDDPYVSG
160 170 180 190 200
LQESYLDQAI GWARNNSLKV WVDLHGAAGS QNGFDNSGLR DSYKFLEDSN
210 220 230 240 250
LAVTTNVLNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM DKMKNDYLAP
260 270 280 290 300
AYEYLRNNIK SDQVIIIHDA FQPYNYWDDF MTENDGYWGV TIDHHHYQVF
310 320 330 340 350
ASDQLERSID EHIKVACEWG TGVLNESHWT VCGEFAAALT DCTKWLNSVG
360 370 380 390 400
FGARYDGSWV NGDQTSSYIG SCANNDDIAY WSDERKENTR RYVEAQLDAF
410 420 430 440
EMRGGWIIWC YKTESSLEWD AQRLMFNGLF PQPLTDRKYP NQCGTISN
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.
InParanoidi P23776.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 140 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