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Q876J3

- EXG_SACU7

UniProt

Q876J3 - EXG_SACU7

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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: 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 sitei232 – 2321Proton donorBy similarity
Active sitei334 – 3341NucleophileBy 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
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

Secreted Curated

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 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 4021Sequence AnalysisPRO_0000007890Add
BLAST
Chaini41 – 448408Glucan 1,3-beta-glucosidasePRO_0000007889Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi317 ↔ 443By similarity
Disulfide bondi342 ↔ 372By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ876J3.
SMRiQ876J3. Positions 41-448.
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

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        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:
EMBL
GenBank
DDBJ
Links Updated
AY144818 Genomic DNA. Translation: AAO32382.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY144818 Genomic DNA. Translation: AAO32382.1 .

3D structure databases

ProteinModelPortali Q876J3.
SMRi Q876J3. Positions 41-448.
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. "Yeast genome duplication was followed by asynchronous differentiation of duplicated genes."
    Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.
    Nature 421:848-852(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 623-6C / CBS 9787 / CLIB 533.

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: 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