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Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550 / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var. uvarum)
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)DescriptionActionsGraphical viewLength
Active sitei232Proton donorBy similarity1
Active sitei334NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

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
OrganismiSaccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550 / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var. uvarum)
Taxonomic identifieri226127 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000000789020 – 40Sequence analysisAdd BLAST21
ChainiPRO_000000788941 – 448Glucan 1,3-beta-glucosidaseAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi317 ↔ 443By similarity
Disulfide bondi342 ↔ 372By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ876J3.
SMRiQ876J3.
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.

Q876J3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLKTLLCT LLTVSSVIAN PVPARDPSSI QFVHEENKKR YYDYDNGALG
60 70 80 90 100
EPIRGVNIGG WLVLEPYITP SLFEAFRTND NNDDGIPVDE YHYCQYLGND
110 120 130 140 150
LAKSRLQSHW STFYQEQDFA NIASQGFNLV RIPIGYWAFA TLDNDPYVTG
160 170 180 190 200
LQESYLDQAI GWARNNSLKV WVDLHGAAGS QNGFDNSGLR DSYEFLEDSN
210 220 230 240 250
LAVTTKALNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM DKMKNDYLLP
260 270 280 290 300
AYEYLRNTIE SNQIIIMHDA FQQFNYWDDF MTETDGYWGV TIDHHHYQVF
310 320 330 340 350
DSSQLESSMD EHIQVACQWG TGVLDEAHWT VCGEFAAALT DCTKWVNSVG
360 370 380 390 400
FGARYDGSWV NGDETSTYIG SCANNDDITS WSDQRKENTR RYVEAQLDAF
410 420 430 440
EMRGGWIIWC YKTESSLEWD VQRLMYNGLF PQPLTDRQYP NQCNTTSS
Length:448
Mass (Da):51,229
Last modified:June 1, 2003 - v1
Checksum:i80AAF86129D16F1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY144818 Genomic DNA. Translation: AAO32382.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY144818 Genomic DNA. Translation: AAO32382.1.

3D structure databases

ProteinModelPortaliQ876J3.
SMRiQ876J3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

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...

Entry informationi

Entry nameiEXG_SACU7
AccessioniPrimary (citable) accession number: Q876J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 59 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

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 one 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.