P23776 (EXG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

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

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.7.
Miscellaneous	Present with 4280 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.

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 Reference proteome
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellular glucan metabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	extracellular region Inferred from direct assay. Source: SGD fungal-type cell wall Inferred from direct assay Ref.7. Source: SGD
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro glucan exo-1,3-beta-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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

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.9

Glycosylation

325

1

N-linked (GlcNAc...) Ref.9

Experimental info

Sequence conflict

41

1

Y → Q AA sequence Ref.7

Sequence conflict

46

1

H → G AA sequence Ref.7

Sequence conflict

77

1

R → H AA sequence Ref.5

Secondary structure

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448

Helix Strand Turn

Details...

Beta strand

53 – 57

5

Beta strand

61 – 63

3

Turn

66 – 68

3

Helix

70 – 74

5

Helix

90 – 97

8

Helix

99 – 113

15

Helix

116 – 124

9

Beta strand

129 – 135

7

Helix

136 – 138

3

Helix

152 – 165

14

Beta strand

169 – 176

8

Helix

185 – 187

3

Helix

198 – 214

17

Helix

218 – 221

4

Beta strand

224 – 229

6

Helix

235 – 237

3

Helix

240 – 246

7

Helix

248 – 257

10

Beta strand

265 – 268

4

Helix

276 – 279

4

Helix

283 – 285

3

Beta strand

289 – 296

8

Helix

302 – 305

4

Helix

309 – 323

15

Beta strand

327 – 335

9

Beta strand

339 – 341

3

Turn

344 – 347

4

Turn

373 – 376

4

Helix

378 – 380

3

Helix

383 – 400

18

Turn

401 – 404

4

Beta strand

405 – 409

5

Helix

421 – 426

6

Helix

442 – 444

3

Sequences

	Sequence		Length	Mass (Da)
	P23776 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: F0AD512E410375BD	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

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. , 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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] 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: 2125957] [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: 8488724] [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: 9748433] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-51, SUBCELLULAR LOCATION. Strain: ATCC 96099 / S288c / SEY6210.
[8]	"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].
[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: 14730348] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 41-448, GLYCOSYLATION AT ASN-165 AND ASN-325.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34341 Genomic DNA. Translation: AAA34599.1.
U17243 Genomic DNA. Translation: AAB67345.1.
AY693069 Genomic DNA. Translation: AAT93088.1.
BK006945 Genomic DNA. Translation: DAA09610.1.

PIR

JN0118.

RefSeq

NP_013403.1. NM_001182188.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P23776.

SMR

P23776. Positions 41-448.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6384N.

IntAct

P23776. 3 interactions.

MINT

MINT-680007.

STRING

P23776.

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

2D gel databases

COMPLUYEAST-2DPAGE

P23776.

Proteomic databases

PeptideAtlas

P23776.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR300W; YLR300W; YLR300W.

GeneID

851007.

KEGG

sce:YLR300W.

NMPDR

fig|4932.3.peg.4421.

Organism-specific databases

CYGD

YLR300w.

SGD

S000004291. EXG1.

Phylogenomic databases

eggNOG

fuNOG04199.

GeneTree

EFGT00050000000564.

HOGENOM

HBG735468.

OMA

WVDLHGA.

OrthoDB

EOG4VX5DT.

Gene expression databases

ArrayExpress

P23776.

Genevestigator

P23776.

GermOnline

YLR300W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

KO

K01210.

Pfam

PF00150. Cellulase. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

967558.

PMAP-CutDB

P23776.

Entry information

Entry name

EXG1_YEAST

Accession

Primary (citable) accession number: P23776
Secondary accession number(s): D6VYU4, Q9UR92

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program