Q9FUK7 (Q9FUK7_HORVU) Unreviewed, UniProtKB/TrEMBL
Last modified
October 19, 2011.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Beta-amylase RuleBase RU000509 EC=3.2.1.2 RuleBase RU000509 |
| Organism | Hordeum vulgare (Barley) EMBL AAG25637.1 |
| 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 | 533 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains. RuleBase RU000509 |
| Sequence similarities | Belongs to the glycosyl hydrolase 14 family. RuleBase RU004157 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Polysaccharide degradation RuleBase RU000509 |
| Molecular function | Glycosidase RuleBase RU000509 Hydrolase |
| Gene Ontology (GO) | |
| Biological process | polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | beta-amylase activity Inferred from electronic annotation. Source: EC cation bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||
Experimental info | ||||||||
|---|---|---|---|---|---|---|---|---|
| Non-terminal residue | 1 | 1 | EMBL AAG25637.1 | |||||
Sequences
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References
| [1] | "The amino acid substitutions of barley beta-amylase that improve thermostability and substrate-binding affinity." Ma Y., Evans E.D., Logue S.J., Langridge P. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF300799 mRNA. Translation: AAG25637.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B1Y based on UniProtKB P16098. |
| ProteinModelPortal | Q9FUK7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9FUK7. 1 interaction. |
Protein family/group databases | |
| CAZy | GH14. Glycoside Hydrolase Family 14. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| Gramene | Q9FUK7. |
Gene expression databases | |
| Genevestigator | Q9FUK7. |
Family and domain databases | |
| InterPro | IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR001371. Glyco_hydro_14B_pln. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| Pfam | PF01373. Glyco_hydro_14. 1 hit. [Graphical view] |
| PRINTS | PR00750. BETAAMYLASE. PR00842. GLHYDLASE14B. |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q9FUK7_HORVU | ||||||||
| Accession | Primary (citable) accession number: Q9FUK7 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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