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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: -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.

Miscellaneous

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

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)DescriptionActionsGraphical viewLength
Active sitei232Proton donorBy similarity1
Active sitei334NucleophileBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • cellular glucan metabolic process Source: SGD
  • fungal-type cell wall organization Source: SGD
  • glucan catabolic process Source: GO_Central

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCell 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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR300W
SGDiS000004291 EXG1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000000789220 – 404 PublicationsAdd BLAST21
ChainiPRO_000000789341 – 448Glucan 1,3-beta-glucosidase I/IIAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi165N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi325N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Proteomic databases

MaxQBiP23776
PaxDbiP23776
PRIDEiP23776

2D gel databases

COMPLUYEAST-2DPAGEP23776

PTM databases

iPTMnetiP23776

Miscellaneous databases

PMAP-CutDBP23776

Interactioni

Protein-protein interaction databases

BioGridi31564, 105 interactors
DIPiDIP-6384N
IntActiP23776, 3 interactors
STRINGi4932.YLR300W

Structurei

Secondary structure

1448
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 57Combined sources5
Beta strandi61 – 63Combined sources3
Turni66 – 68Combined sources3
Helixi70 – 74Combined sources5
Helixi90 – 97Combined sources8
Helixi99 – 113Combined sources15
Helixi116 – 124Combined sources9
Beta strandi129 – 135Combined sources7
Helixi136 – 138Combined sources3
Helixi152 – 165Combined sources14
Beta strandi169 – 176Combined sources8
Helixi185 – 187Combined sources3
Helixi198 – 214Combined sources17
Helixi218 – 221Combined sources4
Beta strandi224 – 229Combined sources6
Helixi235 – 237Combined sources3
Helixi240 – 246Combined sources7
Helixi248 – 257Combined sources10
Beta strandi265 – 268Combined sources4
Helixi276 – 279Combined sources4
Helixi283 – 285Combined sources3
Beta strandi289 – 296Combined sources8
Helixi302 – 305Combined sources4
Helixi309 – 323Combined sources15
Beta strandi327 – 335Combined sources9
Beta strandi339 – 341Combined sources3
Turni344 – 347Combined sources4
Turni373 – 376Combined sources4
Helixi378 – 380Combined sources3
Helixi383 – 400Combined sources18
Turni401 – 404Combined sources4
Beta strandi405 – 409Combined sources5
Helixi421 – 426Combined sources6
Helixi442 – 444Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H4PX-ray1.75A/B41-448[»]
ProteinModelPortaliP23776
SMRiP23776
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23776

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00390000009809
HOGENOMiHOG000114462
InParanoidiP23776
KOiK01210
OMAiYWSVPIT
OrthoDBiEOG092C22A6

Family and domain databases

InterProiView protein in InterPro
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00150 Cellulase, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00659 GLYCOSYL_HYDROL_F5, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti41Y → Q AA sequence (PubMed:9748433).Curated1
Sequence conflicti46H → G AA sequence (PubMed:9748433).Curated1
Sequence conflicti77R → H AA sequence (PubMed:2125957).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiEXG1_YEAST
AccessioniPrimary (citable) accession number: P23776
Secondary accession number(s): D6VYU4, Q9UR92
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: May 23, 2018
This is version 167 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

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