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P29717 (EXG1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan 1,3-beta-glucosidase

EC=2.4.1.-
EC=3.2.1.58
Alternative name(s):
Exo-1,3-beta-glucanase
Gene names
Name:XOG1
Synonyms:EXG, EXG1, XOG
ORF Names:Ca49C10.05, CaO19.10507, CaO19.2990
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major glucan 1,3-beta-glucosidase required for cell wall integrity. Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Can also function biosynthetically as a transglycosylase. Functions to deliver glucan from the cell to the extracellular matrix. Does not appear to impact cell wall glucan content of biofilm cells, nor is it necessary for filamentation or biofilm formation. Involved in cell-substrate and cell-cell adhesion. Adhesion to host-cell surfaces is the first critical step during mucosal infection. XOG1 is target of human antimicrobial peptide LL-37 for inhibition of cell adhesion. Ref.15 Ref.16

Catalytic activity

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose. Ref.6 Ref.15 Ref.20

Enzyme regulation

Binding of human antimicrobial peptide LL-37 decreases the catalytic activity, which leads to the decrease of cell adhesion. Ref.15

Subunit structure

Monomer. Interacts with the human antimicrobial peptide LL-37. Ref.4 Ref.15

Subcellular location

Secretedcell wall. Note: Is non-covalently attached to the cell wall. Ref.4 Ref.9 Ref.11 Ref.13 Ref.14 Ref.17 Ref.18

Induction

Expression is maximal during the early rapid growth phase and increases during biofilm growth. Induced by caspofungin. Transcripts is also regulated by RCK2, SIT4, and HTG4. Ref.7 Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16

Disruption phenotype

Leads to enhanced susceptibility to the commonly used antifungal, fluconazole, during biofilm growth only. Ref.16

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Biophysicochemical properties

Kinetic parameters:

KM=23.0 mM for laminaribiose Ref.6

KM=12.7 mM for laminaritriose

KM=5.0 mM for laminaritetraose

KM=2.6 mM for laminaripentaose

KM=2.7 mM for laminarihexaose

KM=2.4 mM for laminariheptaose

KM=3.9 mM for laminarin

KM=17.9 mM for pustulan

KM=260 mM for gentiobiose

KM=120 mM for gentiotriose

KM=70 mM for cellobiose

KM=9.4 mM for cellotetraose

KM=12.0 mM for cellohexaose

KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG)

Ontologies

Keywords
   Biological processCell adhesion
Cell wall biogenesis/degradation
Virulence
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Transferase
   PTMCleavage on pair of basic residues
Disulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell-substrate adhesion

Inferred from direct assay Ref.15. Source: CGD

cellular glucan metabolic process

Inferred from mutant phenotype Ref.15. Source: CGD

fungal-type cell wall organization

Inferred from mutant phenotype PubMed 9308184. Source: CGD

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

single-species biofilm formation in or on host organism

Inferred from mutant phenotype Ref.16. Source: CGD

single-species biofilm formation on inanimate substrate

Inferred from mutant phenotype Ref.16. Source: CGD

   Cellular_componentanchored component of plasma membrane

Inferred from direct assay PubMed 19824013. Source: CGD

cell surface

Inferred from direct assay Ref.11. Source: CGD

cell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from direct assay Ref.6Ref.4Ref.9Ref.13. Source: CGD

   Molecular_functioncell adhesion molecule binding

Inferred from direct assay Ref.15. Source: CGD

glucan exo-1,3-beta-glucosidase activity

Inferred from direct assay Ref.6Ref.4Ref.5. Source: CGD

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121Or 25 Potential
Propeptide22 – 3817
PRO_0000007878
Chain39 – 438400Glucan 1,3-beta-glucosidase
PRO_0000007879

Sites

Active site2301Proton donor By similarity
Active site3301Nucleophile Ref.5
Binding site651Substrate
Binding site671Substrate
Binding site2301Substrate
Binding site2931Substrate
Binding site3001Substrate

Amino acid modifications

Disulfide bond313 ↔ 435 Ref.19
Disulfide bond338 ↔ 364 Ref.19

Natural variations

Natural variant3671L → M in allele CaO19.10507.

Experimental info

Mutagenesis1821F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296. Ref.20
Mutagenesis2671F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296 or Ser-330. Ref.20
Mutagenesis2961F → A: Impairs catalytic activity; when associated with Ala-182. Ref.20
Mutagenesis2961F → W or I: Decreases catalytic activity. Ref.20
Mutagenesis3301E → Q: Impairs catalytic activity. Ref.20
Mutagenesis3301E → S: Impairs catalytic activity; when associated with Ala-267. Ref.20
Sequence conflict1021S → L in CAA21969. Ref.2
Sequence conflict1931F → S in CAA21969. Ref.2

Secondary structure

.................................................................. 438
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29717 [UniParc].

Last modified March 3, 2009. Version 4.
Checksum: 9BAFEBC484B0121D

FASTA43850,038
        10         20         30         40         50         60 
MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN NVIRGVNLGG 

        70         80         90        100        110        120 
WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA ASRILQKHWS TWITEQDFKQ 

       130        140        150        160        170        180 
ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ VQYLEKALGW ARKNNIRVWI DLHGAPGSQN 

       190        200        210        220        230        240 
GFDNSGLRDS YNFQNGDNTQ VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK 

       250        260        270        280        290        300 
LKQFFLDGYN SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE 

       310        320        330        340        350        360 
LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR YEGAYDNAPY 

       370        380        390        400        410        420 
IGSCQPLLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF WSWKTENAPE WSFQTLTYNG 

       430 
LFPQPVTDRQ FPNQCGFH 

« Hide

References

« Hide 'large scale' references
[1]"An exo-beta-(1,3)-glucanase of Candida albicans: purification of the enzyme and molecular cloning of the gene."
Chambers R.S., Broughton M.J., Cannon R.D., Carne A., Emerson G.W., Sullivan P.A.
J. Gen. Microbiol. 139:325-334(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-73.
Strain: ATCC 10261 / CBS 2718 / NBRC 1061.
[2]"Candida albicans strain 1161 genome pilot sequencing project."
Taylor K., Harris D., Barrell B.G., Rajandream M.A.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE CAO19.10507).
Strain: 1161.
[3]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[4]"The major exoglucanase from Candida albicans: a non-glycosylated secretory monomer related to its counterpart from Saccharomyces cerevisiae."
Luna-Arias J.P., Analuz E., Ridruejo J.C., Olivero I., Larriba G.
Yeast 7:833-841(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-73, SUBCELLULAR LOCATION, SUBUNIT.
Strain: 3153A.
[5]"Identification of Glu-330 as the catalytic nucleophile of Candida albicans exo-beta-(1,3)-glucanase."
MacKenzie L.F., Brooke G.S., Cutfield J.F., Sullivan P.A., Withers S.G.
J. Biol. Chem. 272:3161-3167(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE GLU-330.
[6]"Hydrolase and transferase activities of the beta-1,3-exoglucanase of Candida albicans."
Stubbs H.J., Brasch D.J., Emerson G.W., Sullivan P.A.
Eur. J. Biochem. 263:889-895(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"The serine/threonine protein phosphatase SIT4 modulates yeast-to-hypha morphogenesis and virulence in Candida albicans."
Lee C.M., Nantel A., Jiang L., Whiteway M., Shen S.H.
Mol. Microbiol. 51:691-709(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"A glucose sensor in Candida albicans."
Brown V., Sexton J.A., Johnston M.
Eukaryot. Cell 5:1726-1737(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"Trifluoromethanesulfonic acid-based proteomic analysis of cell wall and secreted proteins of the ascomycetous fungi Neurospora crassa and Candida albicans."
Maddi A., Bowman S.M., Free S.J.
Fungal Genet. Biol. 46:768-781(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[10]"The MAP kinase-activated protein kinase Rck2p regulates cellular responses to cell wall stresses, filamentation and virulence in the human fungal pathogen Candida albicans."
Li X., Du W., Zhao J., Zhang L., Zhu Z., Jiang L.
FEMS Yeast Res. 10:441-451(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"Identification of Candida albicans exposed surface proteins in vivo by a rapid proteomic approach."
Hernaez M.L., Ximenez-Embun P., Martinez-Gomariz M., Gutierrez-Blazquez M.D., Nombela C., Gil C.
J. Proteomics 73:1404-1409(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[12]"Proteomic analysis of proteins released from growth-arrested Candida albicans following exposure to caspofungin."
Kelly J., Kavanagh K.
Med. Mycol. 48:598-605(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
[13]"Mass spectrometric analysis of the secretome of Candida albicans."
Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.
Yeast 27:661-672(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[14]"Effects of fluconazole on the secretome, the wall proteome, and wall integrity of the clinical fungus Candida albicans."
Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G., de Koning L.J., Klis F.M.
Eukaryot. Cell 10:1071-1081(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION.
[15]"Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37."
Tsai P.W., Yang C.Y., Chang H.T., Lan C.Y.
PLoS ONE 6:E21394-E21394(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANTIMICROBIAL PEPTIDE LL-37, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION.
[16]"A Candida biofilm-induced pathway for matrix glucan delivery: implications for drug resistance."
Taff H.T., Nett J.E., Zarnowski R., Ross K.M., Sanchez H., Cain M.T., Hamaker J., Mitchell A.P., Andes D.R.
PLoS Pathog. 8:E1002848-E1002848(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
[17]"Surface stress induces a conserved cell wall stress response in the pathogenic fungus Candida albicans."
Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G., Brul S., de Koning L.J., Klis F.M.
Eukaryot. Cell 12:254-264(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[18]"A family of secreted pathogenesis-related proteins in Candida albicans."
Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D., Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.
Mol. Microbiol. 87:132-151(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[19]"The structure of the exo-beta-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases."
Cutfield S.M., Davies G.J., Murshudov G., Anderson B.F., Moody P.C., Sullivan P.A., Cutfield J.F.
J. Mol. Biol. 294:771-783(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 45-438, DISULFIDE BOND, SUBSTRATE-BINDING.
[20]"Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance."
Patrick W.M., Nakatani Y., Cutfield S.M., Sharpe M.L., Ramsay R.J., Cutfield J.F.
FEBS J. 277:4549-4561(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 39-438 IN COMPLEX WITH SUBSTRATE, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-182; PHE-267; PHE-296 AND GLU-330.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56556 Genomic DNA. Translation: CAA39908.1.
AL033497 Genomic DNA. Translation: CAA21969.1.
AACQ01000015 Genomic DNA. Translation: EAL02690.1.
AACQ01000017 Genomic DNA. Translation: EAL02409.1.
PIRA47702.
T52149.
RefSeqXP_721216.1. XM_716123.1.
XP_721488.1. XM_716395.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZ1X-ray1.85A45-438[»]
1EQCX-ray1.85A45-438[»]
1EQPX-ray1.90A45-438[»]
2PB1X-ray1.90A39-438[»]
2PBOX-ray1.85A39-438[»]
2PC8X-ray1.80A39-438[»]
2PF0X-ray1.90A39-438[»]
3N9KX-ray1.70A40-438[»]
3O6AX-ray2.00A40-438[»]
ProteinModelPortalP29717.
SMRP29717. Positions 45-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0006153.

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.
mycoCLAPEXG5A_CANAL.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3636837.
3637158.
KEGGcal:CaO19.2990.

Phylogenomic databases

eggNOGCOG2730.
KOK01210.
OrthoDBEOG7JT75H.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29717.
PMAP-CutDBP29717.

Entry information

Entry nameEXG1_CANAL
AccessionPrimary (citable) accession number: P29717
Secondary accession number(s): Q5AI63, Q5AIZ3, Q9URL8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 107 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Candida albicans

Candida albicans: entries and gene names