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Protein

Glucan 1,3-beta-glucosidase

Gene

KLLA0C05324g

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei215 – 2151Proton donorBy similarity
Active sitei316 – 3161NucleophileBy 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.
mycoCLAPiEXG5A_KLULA.

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
Ordered Locus Names:KLLA0C05324g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598 Componenti: Chromosome C

Subcellular locationi

Secreted Curated

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 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 278By similarityPRO_0000007884
Chaini28 – 429402Glucan 1,3-beta-glucosidaseBy similarityPRO_0000007885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi299 ↔ 425By similarity
Disulfide bondi324 ↔ 354By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Interactioni

Protein-protein interaction databases

STRINGi28985.Q12628.

Structurei

3D structure databases

ProteinModelPortaliQ12628.
SMRiQ12628. Positions 28-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ12628.
KOiK01210.
OMAiFATIKSW.
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.

Q12628-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSMQVVSLI SLLVSVCLAQ PLPLSKRYFE YENYKVRGVN LGGWLVLEPF
60 70 80 90 100
ITPSLFETFR TNEYNDDGIP YDEYHYCQYL GEDLARDRLK QHWSTWITEA
110 120 130 140 150
DFEDISNTGL NTVRIPIGYW AFELLDDDPY VSGLQEAYLD QAIEWARSYG
160 170 180 190 200
LKVWVDLHGA PGSQNGFDNS GLRDQVEFQQ DGNWDVFKNV LAYVIEKYSR
210 220 230 240 250
DEFTDTVVGV EVLNEPLGPV IDMDKLKELY NWAYDYLRND LQRDQILVIH
260 270 280 290 300
DAFQKANYFD DQLTVEQGAF GVLVDHHHYQ VFSPEEVGRT IDEHISVVCE
310 320 330 340 350
QGKETLTEAH WNVVGEWSAA LTDCTKWLNG VGIGARYDGS FVKNQDTSYW
360 370 380 390 400
IGSCEGSQDI STWTSDKKDN YRKYIEAQLD AYEIRNGWIY WCYKTEDTLE
410 420
WDYRKLVQSG LFPQPLTNRQ FPNQCSSTY
Length:429
Mass (Da):49,811
Last modified:October 31, 1996 - v1
Checksum:i64DA906BCE450B8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46869 Genomic DNA. Translation: CAA86949.1.
CR382123 Genomic DNA. Translation: CAH01288.1.
RefSeqiXP_452437.1. XM_452437.1.

Genome annotation databases

GeneIDi2892517.
KEGGikla:KLLA0C05324g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46869 Genomic DNA. Translation: CAA86949.1.
CR382123 Genomic DNA. Translation: CAH01288.1.
RefSeqiXP_452437.1. XM_452437.1.

3D structure databases

ProteinModelPortaliQ12628.
SMRiQ12628. Positions 28-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi28985.Q12628.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5A_KLULA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2892517.
KEGGikla:KLLA0C05324g.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ12628.
KOiK01210.
OMAiFATIKSW.
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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Entry informationi

Entry nameiEXG_KLULA
AccessioniPrimary (citable) accession number: Q12628
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2004
Last sequence update: October 31, 1996
Last modified: January 6, 2015
This is version 90 of the entry and version 1 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.