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P29717

- EXG1_CANAL

UniProt

P29717 - EXG1_CANAL

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Protein

Glucan 1,3-beta-glucosidase

Gene
XOG1, EXG, EXG1, XOG, Ca49C10.05, CaO19.10507, CaO19.2990
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Binding of human antimicrobial peptide LL-37 decreases the catalytic activity, which leads to the decrease of cell adhesion.1 Publication

Kineticsi

  1. KM=23.0 mM for laminaribiose1 Publication
  2. KM=12.7 mM for laminaritriose
  3. KM=5.0 mM for laminaritetraose
  4. KM=2.6 mM for laminaripentaose
  5. KM=2.7 mM for laminarihexaose
  6. KM=2.4 mM for laminariheptaose
  7. KM=3.9 mM for laminarin
  8. KM=17.9 mM for pustulan
  9. KM=260 mM for gentiobiose
  10. KM=120 mM for gentiotriose
  11. KM=70 mM for cellobiose
  12. KM=9.4 mM for cellotetraose
  13. KM=12.0 mM for cellohexaose
  14. KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651Substrate
Binding sitei67 – 671Substrate
Active sitei230 – 2301Proton donor By similarity
Binding sitei230 – 2301Substrate
Binding sitei293 – 2931Substrate
Binding sitei300 – 3001Substrate
Active sitei330 – 3301Nucleophile1 Publication

GO - Molecular functioni

  1. cell adhesion molecule binding Source: CGD
  2. glucan exo-1,3-beta-glucosidase activity Source: CGD
  3. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell-substrate adhesion Source: CGD
  2. cellular glucan metabolic process Source: CGD
  3. fungal-type cell wall organization Source: CGD
  4. pathogenesis Source: UniProtKB-KW
  5. single-species biofilm formation in or on host organism Source: CGD
  6. single-species biofilm formation on inanimate substrate Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Transferase

Keywords - Biological processi

Cell adhesion, Cell wall biogenesis/degradation, Virulence

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5A_CANAL.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase (EC:2.4.1.-, EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase
Gene namesi
Name:XOG1
Synonyms:EXG, EXG1, XOG
ORF Names:Ca49C10.05, CaO19.10507, CaO19.2990
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
ProteomesiUP000000559: Unassembled WGS sequence

Subcellular locationi

Secretedcell wall
Note: Is non-covalently attached to the cell wall.7 Publications

GO - Cellular componenti

  1. anchored component of plasma membrane Source: CGD
  2. cell surface Source: CGD
  3. cell wall Source: UniProtKB-SubCell
  4. extracellular region Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Disruption phenotypei

Leads to enhanced susceptibility to the commonly used antifungal, fluconazole, during biofilm growth only.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi182 – 1821F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296. 1 Publication
Mutagenesisi267 – 2671F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296 or Ser-330. 1 Publication
Mutagenesisi296 – 2961F → A: Impairs catalytic activity; when associated with Ala-182. 1 Publication
Mutagenesisi296 – 2961F → W or I: Decreases catalytic activity. 1 Publication
Mutagenesisi330 – 3301E → Q: Impairs catalytic activity. 1 Publication
Mutagenesisi330 – 3301E → S: Impairs catalytic activity; when associated with Ala-267. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Or 25 Reviewed predictionAdd
BLAST
Propeptidei22 – 3817PRO_0000007878Add
BLAST
Chaini39 – 438400Glucan 1,3-beta-glucosidasePRO_0000007879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi313 ↔ 4351 Publication
Disulfide bondi338 ↔ 3641 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Miscellaneous databases

PMAP-CutDBP29717.

Expressioni

Inductioni

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 HTG4.7 Publications

Interactioni

Subunit structurei

Monomer. Interacts with the human antimicrobial peptide LL-37.2 Publications

Protein-protein interaction databases

STRINGi5476.CAL0006153.

Structurei

Secondary structure

1
438
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni48 – 503
Beta strandi53 – 575
Beta strandi61 – 633
Turni66 – 683
Helixi70 – 723
Helixi74 – 763
Helixi89 – 11224
Helixi115 – 1239
Beta strandi128 – 1347
Helixi135 – 1373
Helixi150 – 16314
Beta strandi167 – 1748
Helixi183 – 1853
Helixi198 – 21316
Helixi216 – 2183
Turni219 – 2213
Beta strandi222 – 2276
Helixi233 – 2353
Helixi238 – 25417
Beta strandi261 – 2644
Turni270 – 2756
Helixi279 – 2813
Beta strandi285 – 2917
Helixi298 – 3014
Helixi305 – 32016
Beta strandi323 – 3308
Beta strandi335 – 3373
Turni340 – 3434
Helixi365 – 3673
Helixi370 – 3723
Helixi375 – 39319
Turni394 – 3963
Beta strandi397 – 4015
Helixi409 – 4113
Helixi413 – 4186

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP29717.
SMRiP29717. Positions 45-438.

Miscellaneous databases

EvolutionaryTraceiP29717.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
KOiK01210.
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.

P29717-1 [UniParc]FASTAAdd to Basket

« Hide

MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN    50
NVIRGVNLGG WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA 100
ASRILQKHWS TWITEQDFKQ ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ 150
VQYLEKALGW ARKNNIRVWI DLHGAPGSQN GFDNSGLRDS YNFQNGDNTQ 200
VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK LKQFFLDGYN 250
SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE 300
LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR 350
YEGAYDNAPY IGSCQPLLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF 400
WSWKTENAPE WSFQTLTYNG LFPQPVTDRQ FPNQCGFH 438
Length:438
Mass (Da):50,038
Last modified:March 3, 2009 - v4
Checksum:i9BAFEBC484B0121D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti367 – 3671L → M in allele CaO19.10507.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021S → L in CAA21969. 1 Publication
Sequence conflicti193 – 1931F → S in CAA21969. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56556 Genomic DNA. Translation: CAA39908.1.
AL033497 Genomic DNA. Translation: CAA21969.1.
AACQ01000015 Genomic DNA. Translation: EAL02690.1.
AACQ01000017 Genomic DNA. Translation: EAL02409.1.
PIRiA47702.
T52149.
RefSeqiXP_721216.1. XM_716123.1.
XP_721488.1. XM_716395.1.

Genome annotation databases

GeneIDi3636837.
3637158.
KEGGical:CaO19.10507.
cal:CaO19.2990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56556 Genomic DNA. Translation: CAA39908.1 .
AL033497 Genomic DNA. Translation: CAA21969.1 .
AACQ01000015 Genomic DNA. Translation: EAL02690.1 .
AACQ01000017 Genomic DNA. Translation: EAL02409.1 .
PIRi A47702.
T52149.
RefSeqi XP_721216.1. XM_716123.1.
XP_721488.1. XM_716395.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CZ1 X-ray 1.85 A 45-438 [» ]
1EQC X-ray 1.85 A 45-438 [» ]
1EQP X-ray 1.90 A 45-438 [» ]
2PB1 X-ray 1.90 A 39-438 [» ]
2PBO X-ray 1.85 A 39-438 [» ]
2PC8 X-ray 1.80 A 39-438 [» ]
2PF0 X-ray 1.90 A 39-438 [» ]
3N9K X-ray 1.70 A 40-438 [» ]
3O6A X-ray 2.00 A 40-438 [» ]
ProteinModelPortali P29717.
SMRi P29717. Positions 45-438.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5476.CAL0006153.

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.
mycoCLAPi EXG5A_CANAL.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3636837.
3637158.
KEGGi cal:CaO19.10507.
cal:CaO19.2990.

Phylogenomic databases

eggNOGi COG2730.
KOi K01210.
OrthoDBi EOG7JT75H.

Miscellaneous databases

EvolutionaryTracei P29717.
PMAP-CutDB P29717.

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. "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. 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. 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. 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.

Entry informationi

Entry nameiEXG1_CANAL
AccessioniPrimary (citable) accession number: P29717
Secondary accession number(s): Q5AI63, Q5AIZ3, Q9URL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 108 of the entry and version 4 of the sequence. [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

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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