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Protein

Glucan 1,3-beta-glucosidase

Gene

XOG1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: 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 laminaritriose1 Publication
  3. KM=5.0 mM for laminaritetraose1 Publication
  4. KM=2.6 mM for laminaripentaose1 Publication
  5. KM=2.7 mM for laminarihexaose1 Publication
  6. KM=2.4 mM for laminariheptaose1 Publication
  7. KM=3.9 mM for laminarin1 Publication
  8. KM=17.9 mM for pustulan1 Publication
  9. KM=260 mM for gentiobiose1 Publication
  10. KM=120 mM for gentiotriose1 Publication
  11. KM=70 mM for cellobiose1 Publication
  12. KM=9.4 mM for cellotetraose1 Publication
  13. KM=12.0 mM for cellohexaose1 Publication
  14. KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei65Substrate1 Publication1
    Binding sitei67Substrate1 Publication1
    Active sitei230Proton donorBy similarity1
    Binding sitei230Substrate1 Publication1
    Binding sitei293Substrate1 Publication1
    Binding sitei300Substrate1 Publication1
    Active sitei330Nucleophile1 Publication1

    GO - Molecular functioni

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

    GO - Biological processi

    • cell-substrate adhesion Source: CGD
    • cellular glucan metabolic process Source: CGD
    • fungal-type cell wall organization Source: CGD
    • pathogenesis Source: UniProtKB-KW
    • single-species biofilm formation in or on host organism Source: CGD
    • 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

    Enzyme and pathway databases

    BRENDAi3.2.1.58. 1096.

    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.-1 Publication, EC:3.2.1.583 Publications)
    Alternative name(s):
    Exo-1,3-beta-glucanase1 Publication
    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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
    Proteomesi
    • UP000000559 Componenti: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0000190583. XOG1.

    Subcellular locationi

    GO - Cellular componenti

    • cell surface Source: CGD
    • cell wall Source: UniProtKB-SubCell
    • 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)DescriptionActionsGraphical viewLength
    Mutagenesisi182F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296. 1 Publication1
    Mutagenesisi267F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296 or Ser-330. 1 Publication1
    Mutagenesisi296F → A: Impairs catalytic activity; when associated with Ala-182. 1 Publication1
    Mutagenesisi296F → W or I: Decreases catalytic activity. 1 Publication1
    Mutagenesisi330E → Q: Impairs catalytic activity. 1 Publication1
    Mutagenesisi330E → S: Impairs catalytic activity; when associated with Ala-267. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 21Or 25Sequence analysisAdd BLAST21
    PropeptideiPRO_000000787822 – 382 PublicationsAdd BLAST17
    ChainiPRO_000000787939 – 438Glucan 1,3-beta-glucosidaseAdd BLAST400

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi313 ↔ 4351 Publication
    Disulfide bondi338 ↔ 3641 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    PRIDEiP29717.

    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 HTG4.6 Publications

    Interactioni

    Subunit structurei

    Monomer. Interacts with the human antimicrobial peptide LL-37.3 Publications

    GO - Molecular functioni

    • cell adhesion molecule binding Source: CGD

    Structurei

    Secondary structure

    1438
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni48 – 50Combined sources3
    Beta strandi53 – 57Combined sources5
    Beta strandi61 – 63Combined sources3
    Turni66 – 68Combined sources3
    Helixi70 – 72Combined sources3
    Helixi74 – 76Combined sources3
    Helixi89 – 112Combined sources24
    Helixi115 – 123Combined sources9
    Beta strandi128 – 134Combined sources7
    Helixi135 – 137Combined sources3
    Helixi150 – 163Combined sources14
    Beta strandi167 – 174Combined sources8
    Helixi183 – 185Combined sources3
    Helixi198 – 213Combined sources16
    Helixi216 – 218Combined sources3
    Turni219 – 221Combined sources3
    Beta strandi222 – 227Combined sources6
    Helixi233 – 235Combined sources3
    Helixi238 – 254Combined sources17
    Beta strandi261 – 264Combined sources4
    Turni270 – 275Combined sources6
    Helixi279 – 281Combined sources3
    Beta strandi285 – 292Combined sources8
    Helixi298 – 301Combined sources4
    Helixi305 – 321Combined sources17
    Beta strandi323 – 331Combined sources9
    Beta strandi335 – 337Combined sources3
    Turni340 – 343Combined sources4
    Helixi365 – 367Combined sources3
    Helixi370 – 372Combined sources3
    Helixi375 – 393Combined sources19
    Turni394 – 396Combined sources3
    Beta strandi397 – 401Combined sources5
    Helixi409 – 411Combined sources3
    Helixi413 – 418Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4M80X-ray1.86A40-438[»]
    4M81X-ray1.86A40-438[»]
    4M82X-ray1.59A40-438[»]
    ProteinModelPortaliP29717.
    SMRiP29717.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29717.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000114462.
    InParanoidiP29717.
    KOiK01210.
    OrthoDBiEOG092C22A6.

    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

            10         20         30         40         50
    MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN
    60 70 80 90 100
    NVIRGVNLGG WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA
    110 120 130 140 150
    ASRILQKHWS TWITEQDFKQ ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ
    160 170 180 190 200
    VQYLEKALGW ARKNNIRVWI DLHGAPGSQN GFDNSGLRDS YNFQNGDNTQ
    210 220 230 240 250
    VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK LKQFFLDGYN
    260 270 280 290 300
    SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE
    310 320 330 340 350
    LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR
    360 370 380 390 400
    YEGAYDNAPY IGSCQPLLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF
    410 420 430
    WSWKTENAPE WSFQTLTYNG LFPQPVTDRQ FPNQCGFH
    Length:438
    Mass (Da):50,038
    Last modified:March 3, 2009 - v4
    Checksum:i9BAFEBC484B0121D
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti102S → L in CAA21969 (Ref. 2) Curated1
    Sequence conflicti193F → S in CAA21969 (Ref. 2) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti367L → M in allele CaO19.10507. 1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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

    EnsemblFungiiEAL02409; EAL02409; CaO19.10507.
    EAL02690; EAL02690; CaO19.2990.
    GeneIDi3636837.
    3637158.
    KEGGical:CaO19.10507.
    cal:CaO19.2990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4M80X-ray1.86A40-438[»]
    4M81X-ray1.86A40-438[»]
    4M82X-ray1.59A40-438[»]
    ProteinModelPortaliP29717.
    SMRiP29717.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEXG5A_CANAL.

    Proteomic databases

    PRIDEiP29717.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiEAL02409; EAL02409; CaO19.10507.
    EAL02690; EAL02690; CaO19.2990.
    GeneIDi3636837.
    3637158.
    KEGGical:CaO19.10507.
    cal:CaO19.2990.

    Organism-specific databases

    CGDiCAL0000190583. XOG1.

    Phylogenomic databases

    HOGENOMiHOG000114462.
    InParanoidiP29717.
    KOiK01210.
    OrthoDBiEOG092C22A6.

    Enzyme and pathway databases

    BRENDAi3.2.1.58. 1096.

    Miscellaneous databases

    EvolutionaryTraceiP29717.
    PMAP-CutDBP29717.

    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]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 124 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.