Glucan 1,3-beta-glucosidase precursor - Candida albicans (Yeast)

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Reviewed, UniProtKB/Swiss-Prot P29717 (EXG_CANAL)

Last modified June 16, 2009. Version 72. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended 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

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro glucan 1,3-beta-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Or 25 Potential

Propeptide

22 – 38

Ref.1 Ref.3

PRO_0000007878

Chain

39 – 438

400

Glucan 1,3-beta-glucosidase

PRO_0000007879

Sites

Active site

230

Proton donor By similarity

Active site

330

Nucleophile Ref.4

Amino acid modifications

Disulfide bond

313 ↔ 435

Disulfide bond

338 ↔ 364

Experimental info

Mutagenesis

330

E → Q: Loss of activity.

Sequence conflict

102

S → L in CAA21969. Ref.2

Sequence conflict

193

F → S in CAA21969. Ref.2

Sequence conflict

367

L → M in CAA21969. Ref.2

Secondary structure

438

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P29717-1 [UniParc].

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

438

50,038

        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

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References

	« Hide 'large scale' referencesShow '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: 8436950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-73. Strain: ATCC 10261 / CBS 2718 / IFO 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 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: 1789004] [Abstract] Cited for: PROTEIN SEQUENCE OF 39-73. Strain: 3153A.
[4]	"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: 9013549] [Abstract] Cited for: ACTIVE SITE GLU-330.
[5]	"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: 10610795] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 45-438.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X56556 Genomic DNA. Translation: CAA39908.1.
AL033497 Genomic DNA. Translation: CAA21969.1.
AACQ01000015 Genomic DNA. Translation: EAL02690.1.

PIR

A47702.
T52149.

RefSeq

XP_721488.1.

3D structure databases

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	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

Genome annotation databases

GeneID

3636837.

Phylogenomic databases

OMA

P29717. WFVLEPY.

Enzyme and pathway databases

BRENDA

3.2.1.58. 1124.

Family and domain databases

InterPro

IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

PMAP-CutDB

P29717.

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Entry information

Entry name

EXG_CANAL

Accession

Primary (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:	June 16, 2009
This is version 72 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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