Glucan 1,3-beta-glucosidase I/II precursor - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

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 names

Name:	EXG1
Synonyms:	BGL1, SCW6
Ordered Locus Names:	YLR300W
ORF Names:	L8003.3

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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 activity	Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.
Subcellular location	Secreted › cell wall. Secreted. Ref.6
Miscellaneous	Present with 4280 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.

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Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Cleavage on pair of basic residues Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellular glucan metabolic process Inferred from genetic interaction. Source: SGD
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell fungal-type cell wall Ref.6 Inferred from direct assay. Source: SGD
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro glucan 1,3-beta-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Propeptide

20 – 40

21

Ref.6 Ref.1 Ref.4 Ref.5

PRO_0000007892

Chain

41 – 448

408

Glucan 1,3-beta-glucosidase I/II

PRO_0000007893

Sites

Active site

232

1

Proton donor By similarity

Active site

334

1

Nucleophile By similarity

Amino acid modifications

Glycosylation

165

1

N-linked (GlcNAc...) Ref.8

Glycosylation

325

1

N-linked (GlcNAc...) Ref.8

Experimental info

Sequence conflict

41

1

Y → Q AA sequence Ref.6

Sequence conflict

46

1

H → G AA sequence Ref.6

Sequence conflict

77

1

R → H AA sequence Ref.4

Secondary structure

1

.

448

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P23776-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: F0AD512E410375BD
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FASTA

448

51,311

        10         20         30         40         50         60 
MLSLKTLLCT LLTVSSVLAT PVPARDPSSI QFVHEENKKR YYDYDHGSLG EPIRGVNIGG 

        70         80         90        100        110        120 
WLLLEPYITP SLFEAFRTND DNDEGIPVDE YHFCQYLGKD LAKSRLQSHW STFYQEQDFA 

       130        140        150        160        170        180 
NIASQGFNLV RIPIGYWAFQ TLDDDPYVSG LQESYLDQAI GWARNNSLKV WVDLHGAAGS 

       190        200        210        220        230        240 
QNGFDNSGLR DSYKFLEDSN LAVTTNVLNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM 

       250        260        270        280        290        300 
DKMKNDYLAP AYEYLRNNIK SDQVIIIHDA FQPYNYWDDF MTENDGYWGV TIDHHHYQVF 

       310        320        330        340        350        360 
ASDQLERSID EHIKVACEWG TGVLNESHWT VCGEFAAALT DCTKWLNSVG FGARYDGSWV 

       370        380        390        400        410        420 
NGDQTSSYIG SCANNDDIAY WSDERKENTR RYVEAQLDAF EMRGGWIIWC YKTESSLEWD 

       430        440 
AQRLMFNGLF PQPLTDRKYP NQCGTISN

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1900250] [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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 2125957] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-86.
[5]	"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: 8488724] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-65.
[6]	"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: 9748433] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-51, SUBCELLULAR LOCATION. Strain: ATCC 96099 / S288c / SEY6210.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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: 14730348] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 41-448, GLYCOSYLATION AT ASN-165 AND ASN-325.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M34341 Genomic DNA. Translation: AAA34599.1.
U17243 Genomic DNA. Translation: AAB67345.1.
AY693069 Genomic DNA. Translation: AAT93088.1.

PIR

JN0118.

RefSeq

NP_013403.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H4P	X-ray	1.75	A/B	41-448	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6384N.

IntAct

P23776. 3 interactions.

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

2-D gel databases

COMPLUYEAST-2DPAGE

P23776.

Proteomic databases

PeptideAtlas

P23776.

Genome annotation databases

Ensembl

YLR300W. Saccharomyces cerevisiae. [Contig view]

GeneID

851007.

GenomeReviews

Gene locus YLR300W in contig Y13138_GR.

KEGG

sce:YLR300W.

NMPDR

fig|4932.3.peg.4421.

Organism-specific databases

CYGD

YLR300w.

SGD

S000004291. EXG1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P23776.

OMA

P23776. WFVLEPY.

Enzyme and pathway databases

BRENDA

3.2.1.58. 250.

Gene expression databases

GermOnline

YLR300W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00150. Cellulase. 1 hit.
[Graphical view]

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

967558.

PMAP-CutDB

P23776.

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Entry information

Entry name

EXG1_YEAST

Accession

Primary (citable) accession number: P23776
Secondary accession number(s): Q9UR92

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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