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Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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 sitei213 – 2131Proton donorBy similarity
Active sitei313 – 3131NucleophileBy 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.

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
Ordered Locus Names:YALI0F05390g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
ProteomesiUP000001300: Chromosome F

Subcellular locationi

Secreted By similarity

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 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 421406Glucan 1,3-beta-glucosidasePRO_0000007888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi296 ↔ 419By similarity
Disulfide bondi321 ↔ 347By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi4952.Q12725.

Structurei

3D structure databases

ProteinModelPortaliQ12725.
SMRiQ12725. Positions 29-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ12725.
KOiK01210.
OMAiNEPNIPG.
OrthoDBiEOG7JT75H.

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.

Q12725-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLTKLVALA GAALASPIQL VPREGSFLGF NYGSEKVHGV NLGGWFVLEP
60 70 80 90 100
FITPSLFEAF GNNDANVPVD EYHYTAWLGK EEAEKRLTDH WNTWITEYDI
110 120 130 140 150
KAIAENYKLN LVRIPIGYWA FSLLPNDPYV QGQEAYLDRA LGWCRKYGVK
160 170 180 190 200
AWVDVHGVPG SQNGFDNSGL RDHWDWPNAD NVQHSINVIN YIAGKYGAPE
210 220 230 240 250
YNDIVVGIEL VNEPLGPAIG MEVIEKYFQE GFWTVRHAGS DTAVVIHDAF
260 270 280 290 300
QEKNYFNNFM TTEQGFWNVV LDHHQYQVFS PGELARNIDQ HIAEVCNVGR
310 320 330 340 350
QASTEYHWRI FGEWSAALTD CTHWLNGVGK GPRLDGSFPG SYYQRSCQGR
360 370 380 390 400
GDIQTWSEQD KQESRRYVEA QLDAWEHGGD GWIYWTYKTE NALEWDFRRL
410 420
VDNGIFPFPY WDRQFPNQCG F
Length:421
Mass (Da):48,275
Last modified:October 11, 2004 - v2
Checksum:i2BB03184758252CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 3331R → S in CAA86952. (PubMed:10029988)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46872 Genomic DNA. Translation: CAA86952.1.
CR382132 Genomic DNA. Translation: CAG77837.1.
RefSeqiXP_505030.1. XM_505030.1.

Genome annotation databases

EnsemblFungiiCAG77837; CAG77837; YALI0_F05390g.
GeneIDi2908269.
KEGGiyli:YALI0F05390g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46872 Genomic DNA. Translation: CAA86952.1.
CR382132 Genomic DNA. Translation: CAG77837.1.
RefSeqiXP_505030.1. XM_505030.1.

3D structure databases

ProteinModelPortaliQ12725.
SMRiQ12725. Positions 29-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4952.Q12725.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG77837; CAG77837; YALI0_F05390g.
GeneIDi2908269.
KEGGiyli:YALI0F05390g.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ12725.
KOiK01210.
OMAiNEPNIPG.
OrthoDBiEOG7JT75H.

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

« Hide 'large scale' publications
  1. "Cloning and characterization of 1,3-beta-glucanase-encoding genes from non-conventional yeasts."
    Esteban P.F., Vazquez de Aldana C.R., del Rey F.
    Yeast 15:91-109(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 20460 / W29 / CBS 7504 / IFP29.
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CLIB 122 / E 150.

Entry informationi

Entry nameiEXG_YARLI
AccessioniPrimary (citable) accession number: Q12725
Secondary accession number(s): Q6C2T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 11, 2004
Last modified: January 7, 2015
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.