Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Candida oleophila (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei214 – 2141Proton donorBy similarity
Active sitei328 – 3281NucleophileBy similarity

GO - Molecular functioni

  1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. cell wall organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5A_CANOL.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase
Gene namesi
Name:EXG1
OrganismiCandida oleophila (Yeast)
Taxonomic identifieri45573 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeKurtzmaniellaKurtzmaniella/Candida clade

Subcellular locationi

  1. Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 425408Glucan 1,3-beta-glucosidasePRO_0000007880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi301 ↔ 423By similarity
Disulfide bondi326 ↔ 352By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ8NKF9.
SMRiQ8NKF9. Positions 30-425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

Q8NKF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLTFAPIFL LISSIVAAPT LQLQRKGLEW DYQNDKIRGV NLGGWFVLEP
60 70 80 90 100
YITPSLFSVW SNGEDDLNTP VDEYHYTQKL GKETALSRLE AHWSSWYTEA
110 120 130 140 150
DFAQMKYLGI NAVRIPIGYW AFQLLDNDPY VQGQVKYLDQ ALEWCRNNGL
160 170 180 190 200
YAWVDLHGAP GSQNGFDNSG LRDSYKFQDD DDVKVTLEVL KTIGAKYGGS
210 220 230 240 250
DYEDVVIGIE LLNEPLGPVL DMDGLRQFYQ DGYSEIRNND GVESYNAIII
260 270 280 290 300
HDAFQQTDHY WDNFMQVSGG YWNVVVDHHH YQVFDQAALE LLIEDHIKTA
310 320 330 340 350
CNWGTTHKDE AHWNIVGEWS SALTDCAKWL NGVGHGARWS GNYDNCPYID
360 370 380 390 400
SCLSYTDLSG WTDEYKTNVR KYTEAQLDAW EQVGGWFFWC WKTESAPEWD
410 420
FQALTNAGLI PQPLNDRQYP NQCGY
Length:425
Mass (Da):48,774
Last modified:October 1, 2002 - v1
Checksum:iC374EB3438AD5D1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF393806 Genomic DNA. Translation: AAM21469.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF393806 Genomic DNA. Translation: AAM21469.1.

3D structure databases

ProteinModelPortaliQ8NKF9.
SMRiQ8NKF9. Positions 30-425.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5A_CANOL.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

Publicationsi

  1. "Cloning and analysis of CoEXG1, a secreted 1,3-beta-glucanase of the yeast biocontrol agent Candida oleophila."
    Segal E., Yehuda H., Droby S., Wisniewski M., Goldway M.
    Yeast 19:1171-1182(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    Strain: ATCC MYA-1208 / I-182 / NRRL Y-18846.

Entry informationi

Entry nameiEXG_CANOL
AccessioniPrimary (citable) accession number: Q8NKF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2002
Last modified: January 7, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.