P83252 (BGAL_HORVU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 33.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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: |
| 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 | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | beta-galactosidase activity Non-traceable author statement Ref.1. Source: UniProtKB cation bindingInferred from electronic annotation. Source: InterPro |
| 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
3D structure databases | |
|---|---|
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| Gramene | P83252. |
Gene expression databases | |
| Genevestigator | P83252. |
Family and domain databases | |
| InterPro | IPR013781. Glyco_hydro_subgr_catalytic. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS01182. GLYCOSYL_HYDROL_F35. Partial match. [Graphical view] |
| ProtoNet | Search... |
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 program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with