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O93983

- EXG2_HANAN

UniProt

O93983 - EXG2_HANAN

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Protein

Glucan 1,3-beta-glucosidase 2

Gene
EXG2
Organism
Hansenula anomala (Yeast) (Candida pelliculosa)
Status
Reviewed - Annotation score: 2 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.

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 sitei217 – 2171Proton donor By similarity
Active sitei316 – 3161Nucleophile By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
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 2 (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase 2
Gene namesi
Name:EXG2
OrganismiHansenula anomala (Yeast) (Candida pelliculosa)
Taxonomic identifieri4927 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeWickerhamomyces

Subcellular locationi

Secreted Reviewed prediction

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 – 1717 Reviewed predictionAdd
BLAST
Chaini18 – 427410Glucan 1,3-beta-glucosidase 2PRO_0000007883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi299 ↔ 426 By similarity
Disulfide bondi324 ↔ 355 By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliO93983.
SMRiO93983. Positions 35-426.

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.

O93983-1 [UniParc]FASTAAdd to Basket

« Hide

MLISTFIISS LLSIALANPI PSRGGTQFYK RGDYWDYQND KIRGVNLGGW    50
FVLEPFITPS LFEAFENQGQ DVPVDEYHYT KALGKDLAKE RLDQHWSSWI 100
VEADFQSIAG AGLNFVRIPI GYWAFQLLDN DPYVQGQESY LDQALEWAKK 150
YDIKVWIDLH GAPGSQNGFD NSGLRDSYEF QNGDNTQVAL DVLQYISNKY 200
GGSDYGDVVI GIELLNEPLG SVLDMGKLND FWQQGYHNLR NTGSSQNVII 250
HDAFQTWDSF NDKFHTPDYW NVVIDHHHYQ VFSPGELSRS VDEHVKVACE 300
WGANSTKENH WNLCGEWSAA MTDCTKWLNG VGRGSRYDQT FDYDPSQNQN 350
YIGSCQGSQD ISTWDDDKKS NYRRYIEAQL DAFEKRSGWI FWTWKTETTL 400
EWDFQKLSYY GIFPSPLTSR QYPGQCD 427
Length:427
Mass (Da):49,130
Last modified:May 1, 1999 - v1
Checksum:iEDF7865B08538BE2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ222862 Genomic DNA. Translation: CAA11018.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ222862 Genomic DNA. Translation: CAA11018.1 .

3D structure databases

ProteinModelPortali O93983.
SMRi O93983. Positions 35-426.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

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. "Preliminary study of exo-beta-1,3-glucanase encoding genes in relation to the protective activity of Pichia anomala (strain K) against Botrytis cinerea on postharvest apples."
    Grevesse C., Jijakli M.H., Duterme O., Colinet D., Lepoivre P.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K.

Entry informationi

Entry nameiEXG2_HANAN
AccessioniPrimary (citable) accession number: O93983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 1999
Last modified: October 16, 2013
This is version 58 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

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