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Protein
Submitted name:

1,3-beta-D-glucan glucanohydrolase (Glucan endo-1,3-beta-glucosidase a)

Gene

gluB20-2

Organism
Solanum tuberosum (Potato)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.39. 5757.

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Submitted name:
1,3-beta-D-glucan glucanohydrolase (Glucan endo-1,3-beta-glucosidase a)Imported (EC:3.2.1.39Imported)
Gene namesi
Name:gluB20-2Imported
OrganismiSolanum tuberosum (Potato)Imported
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 PotentialImportedAdd
BLAST
Chaini24 – 3383151,3-beta-D-glucan glucanohydrolaseImportedPRO_5000072206Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UR7X-ray1.40A/B24-338[»]
3UR8X-ray1.26A/B24-338[»]
4GZIX-ray1.68A24-338[»]
4GZJX-ray1.55A24-338[»]
ProteinModelPortaliQ70C53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.UniRule annotation

Keywords - Domaini

SignalImported

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q70C53-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLSSLVVS LLLVGLLIQI TGAQPIGVCY GKIANNLPSD QDVIKLYNAN
60 70 80 90 100
NIKKMRIYYP HTNVFNALKG SNIEIILDVP NQDLEALANP SNANGWVQDN
110 120 130 140 150
IRNHFPDVKF KYIAVGNEVD PGRESGKYAR FVGPAMENIY NALSSAGLQN
160 170 180 190 200
QIKVSTSTYS GLLTNTYPPR DSIFREEYKS FINPIIGFLA RHNLPLLANI
210 220 230 240 250
YPYFGHIDNT NAVPLSYALF NQQRRNDTGY QNLFDALVDS MYFATEKLGG
260 270 280 290 300
QNIEIIVSES GWPSEGHPAA TLKNARTYYT NLINHVKRGA GTPKKPGKTI
310 320 330
ETYLFAMFDE NEKKGEASEK HFGLFNPDQR PKYQLNFN
Length:338
Mass (Da):37,855
Last modified:July 5, 2004 - v1
Checksum:iA5337C9AF69DF3AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ586575 mRNA. Translation: CAE52322.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ586575 mRNA. Translation: CAE52322.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UR7X-ray1.40A/B24-338[»]
3UR8X-ray1.26A/B24-338[»]
4GZIX-ray1.68A24-338[»]
4GZJX-ray1.55A24-338[»]
ProteinModelPortaliQ70C53.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.39. 5757.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of dual function of 1,3-beta-glucanase product of gluB20-2 gene isolated from potato plants."
    Barabasz A., Krzymowska M., Bieniak B., Charzynska M., Hennig J.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: LeafImported.
  2. "Functional analysis of the 1,3-beta-glucanase, product of gluB20-2 gene in potato."
    Barabasz A.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: LeafImported.
  3. "Two high-resolution structures of potato endo-1,3-beta-glucanase reveal subdomain flexibility with implications for substrate binding."
    Wojtkowiak A., Witek K., Hennig J., Jaskolski M.
    Acta Crystallogr. D 68:713-723(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 24-338.
  4. "Structures of an active-site mutant of a plant 1,3-beta-glucanase in complex with oligosaccharide products of hydrolysis."
    Wojtkowiak A., Witek K., Hennig J., Jaskolski M.
    Acta Crystallogr. D 69:52-62(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 24-338.

Entry informationi

Entry nameiQ70C53_SOLTU
AccessioniPrimary (citable) accession number: Q70C53
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.