Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12700

- EXG_SCHOC

UniProt

Q12700 - EXG_SCHOC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glucan 1,3-beta-glucosidase

Gene
N/A
Organism
Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
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).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 sitei219 – 2191Proton donorBy similarity
Active sitei318 – 3181NucleophileBy 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_DEBOC.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase
OrganismiSchwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
Taxonomic identifieri27300 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeSchwanniomyces

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
Chaini20 – 425406Glucan 1,3-beta-glucosidasePRO_0000007881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi301 ↔ 423By similarity
Disulfide bondi326 ↔ 352By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ12700.
SMRiQ12700. Positions 35-425.
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.

Q12700-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLTLLLLAL IFSPSLIFSL PTANKVKLVK KGLNWDYQNA KIHGVNLGGW
60 70 80 90 100
FVLEPFITPS LFDIYSKPND DSQVPVDEYH FTQKLGKDAA QQVLEQHWKT
110 120 130 140 150
WYKENDFKMM LKYGLNAVRI PIGYWAFKLL DYDPYVQGQV KYLDRALDWA
160 170 180 190 200
RKYNLKVWID LHGAPGSQNG FDNSGLRDSL GFQQGNNVNF TLEVLEIIGK
210 220 230 240 250
KYGGPEYEDV VIGIELLNEP LGPSLDLNYL KEFFQQGYQN LRNSGSVQAV
260 270 280 290 300
IIQDAFQPMG YWDNFLTLDQ YWNVVVDHHH YQVFSAGELQ RSIDDHITVA
310 320 330 340 350
CNWGWDAKKE YHWNVAGEWS AALTDCARWL NGVGRGARFS GDFDNSPYFG
360 370 380 390 400
SCDCYVNIAT WPSEYRTNVR RYIEAQLDAF EQTGGWFFWN WKCENAIEWD
410 420
LQGLITAGVF PYPFYNRQFP NQCGF
Length:425
Mass (Da):49,127
Last modified:November 1, 1996 - v1
Checksum:i57F063ABE2FBF274
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46871 Genomic DNA. Translation: CAA86951.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46871 Genomic DNA. Translation: CAA86951.1 .

3D structure databases

ProteinModelPortali Q12700.
SMRi Q12700. Positions 35-425.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.
mycoCLAPi EXG5A_DEBOC.

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. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26077 / CBS 2863 / JCM 8124 / BCRC 20332 / NBRC 1840 / NRRL Y-2477.

Entry informationi

Entry nameiEXG_SCHOC
AccessioniPrimary (citable) accession number: Q12700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 69 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