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Q875R9

- EXG_LACK1

UniProt

Q875R9 - EXG_LACK1

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Protein
Glucan 1,3-beta-glucosidase
Gene
EXG1
Organism
Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / CCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri)
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 sitei227 – 2271Proton donor By similarity
Active sitei328 – 3281Nucleophile By similarity

GO - Molecular functioni

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

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 (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase
Gene namesi
Name:EXG1
OrganismiLachancea kluyveri (strain ATCC 58438 / CBS 3082 / CCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri)
Taxonomic identifieri226302 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

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 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 439421Glucan 1,3-beta-glucosidase
PRO_0000007891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi311 ↔ 437 By similarity
Disulfide bondi336 ↔ 366 By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ875R9.
SMRiQ875R9. Positions 40-438.

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.

Q875R9-1 [UniParc]FASTAAdd to Basket

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MLLSLLFLLS TFAFGALTQP VPAKSENNVQ FLHSKNKKRF YDYSTELIRG    50
VNIGGWLLLE PYITPSLFEA FRTDENSDAG IPVDEYHYCE ALGSEVAESR 100
LEAHWSTFYT EQDFKNIASA GLNMVRIPIG YWAFKTLDSD PYVTGKQESY 150
LDKAIQWSKD AGLKVWVDLH GAPGSQNGFD NSGLRDHWSF LEDENLNLTK 200
EVIKYLLEKY SREEYLDTVI GIELINEPLG PVLDMDKLKE YYQFGYDYLR 250
NELGSDQIVV IHDAFEAYNY WDSTLTVEDG SWGVVVDHHH YQCFSSDQLA 300
RSIDEHVSVA CEWGTGVLTE SHWTVAGEWS AALTDCAKWI NGVGYGARYD 350
GSFTKDSESS YYIGSCENNE DVSTWSEERK SNNRKYVEAQ LDAFELRGGW 400
IFWCYKTETT VEWDLQRLMY SGLFPQPVTD RQYPNQCGF 439
Length:439
Mass (Da):50,349
Last modified:June 1, 2003 - v1
Checksum:i7EFCB8E266C92729
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145000 Genomic DNA. Translation: AAO32563.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY145000 Genomic DNA. Translation: AAO32563.1 .

3D structure databases

ProteinModelPortali Q875R9.
SMRi Q875R9. Positions 40-438.
ModBasei 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: ATCC 58438 / CBS 3082 / CCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651.

Entry informationi

Entry nameiEXG_LACK1
AccessioniPrimary (citable) accession number: Q875R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: October 16, 2013
This is version 55 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

Similar proteinsi