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P29717 (EXG_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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=3.2.1.58
Alternative name(s):
Exo-1,3-beta-glucanase
Gene names
Name:XOG1
Synonyms:XOG
ORF Names:Ca49C10.05, CaO19.2990
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida ›

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

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. 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.

Subunit structure

Monomer.

Subcellular location

Secreted.

Developmental stage

Maximum expression during the early rapid growth phase.

Sequence similarities

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

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

Amino acid modifications

Disulfide bond313 ↔ 435
Disulfide bond338 ↔ 364

Experimental info

Mutagenesis3301E → Q: Loss of activity.
Sequence conflict1021S → L in CAA21969. Ref.2
Sequence conflict1931F → S in CAA21969. Ref.2
Sequence conflict3671L → M in CAA21969. Ref.2

Secondary structure

1 .................................................................. 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].
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.
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]"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.
+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.
PIRA47702.
T52149.
RefSeqXP_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...

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.
KEGGcal:CaO19.2990.

Phylogenomic databases

eggNOGCOG2730.
KOK01210.

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. Glyco_hydro_cat. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29717.
PMAP-CutDBP29717.

Entry information

Entry nameEXG_CANAL
AccessionPrimary (citable) accession number: P29717
Secondary accession number(s): Q5AIZ3, Q9URL8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 101 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents