Skip Header

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

Q8NKF9

- EXG_CANOL

UniProt

Q8NKF9 - EXG_CANOL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Candida oleophila (Yeast)
Status
Reviewed - 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

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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:
EMBL
GenBank
DDBJ
Links Updated
AF393806 Genomic DNA. Translation: AAM21469.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF393806 Genomic DNA. Translation: AAM21469.1 .

3D structure databases

ProteinModelPortali Q8NKF9.
SMRi Q8NKF9. Positions 30-425.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.
mycoCLAPi EXG5A_CANOL.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  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: October 29, 2014
This is version 54 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