Reviewed,
UniProtKB/Swiss-Prot P83252 (BGAL_HORVU)
Last modified
January 19, 2010.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Beta-galactosidase EC=3.2.1.23 Alternative name(s): Acid beta-galactosidase Short name=Lactase Exo-(1-->4)-beta-D-galactanase Cleaved into the following 2 chains: 1- Recommended name: Beta-galactosidase large subunit 2- Recommended name: Beta-galactosidase small subunit |
| Organism | Hordeum vulgare (Barley) |
| Taxonomic identifier | 4513 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum |
Protein attributes
| Sequence length | 38 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in cell wall degradation. Degrades polysaccharides containing beta-(1-->4)-linked galactans, acting as an exo-(1-->4)-beta-D-galactanase By similarity. UniProtKB P48981 |
| Catalytic activity | Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. UniProtKB P48981 |
| Subunit structure | Heterodimer of a large and a small subunit. Ref.1 |
| Post-translational modification | The small subunit is N-glycosylated. Ref.1 |
| Miscellaneous | There are three forms of the large subunit which have the same sequence but differ in charge. There are four forms of the small subunit which have the same sequence but differ in charge. Ref.1 |
| Sequence similarities | Belongs to the glycosyl hydrolase 35 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | beta-galactosidase activity Ref.1 Non-traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Barley beta-galactosidase: structure, function, heterogeneity, and gene origin." Triantafillidou D., Georgatsos J.G. J. Protein Chem. 20:551-562(2001) [PubMed: 11838543] [Abstract] Cited for: PROTEIN SEQUENCE, SUBUNIT, GLYCOSYLATION. Strain: cv. Sofia. Tissue: Seed. |
Cross-references
Entry information
| Entry name | BGAL_HORVU | ||||||||
| Accession | Primary (citable) accession number: P83252 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


