Reviewed,
UniProtKB/Swiss-Prot Q04524 (ILVB_KLETE)
Last modified
June 16, 2009.
Version 55.
History...
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90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Acetolactate synthase, catabolic Short name=ALS EC=2.2.1.6 | ||
| Gene names |
| ||
| Organism | Klebsiella terrigena (Raoultella terrigena) | ||
| Taxonomic identifier | 577 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Raoultella |
Protein attributes
| Sequence length | 559 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 pyruvate = 2-acetolactate + CO2. |
| Pathway | Polyol metabolism; 2,3-butanediol biosynthesis; (R,R)-2,3-butanediol from pyruvate: step 1/3. |
| Subunit structure | Homodimer. |
| Miscellaneous | Does not seem to require thiamine pyrophosphate By similarity. |
| Sequence similarities | Belongs to the TPP enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate |
| Molecular function | Transferase |
| Gene Ontology (GO) | |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro acetolactate synthase activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW thiamin pyrophosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 559 | 559 | Acetolactate synthase, catabolic | PRO_0000090798 | |||||
Regions | |||||||||
| Nucleotide binding | 263 – 284 | 22 | FAD By similarity | ||||||
| Nucleotide binding | 304 – 323 | 20 | FAD By similarity | ||||||
Sites | |||||||||
| Metal binding | 447 | 1 | Magnesium By similarity | ||||||
| Binding site | 159 | 1 | FAD By similarity | ||||||
Sequences
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References
| [1] | "Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes." Blomqvist K., Nikkola M., Lehtovaara P., Suihko M.-L., Airaksinen U., Straby K.B., Knowles J.K.C., Penttilae M.E. J. Bacteriol. 175:1392-1404(1993) [PubMed: 8444801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VTT-E-74023. |
Cross-references
Sequence databases | |
|---|---|
| L04507 Genomic DNA. Translation: AAA25055.1. | |
| PIR | D47069. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JSC based on UniProtKB P07342. |
| SMR | Q04524. Positions 8-558. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.2.1.6. 3066. |
Family and domain databases | |
| InterPro | IPR012782. Acetolactate_synth_catblc. IPR000399. TPP_bd_CS. IPR012001. TPP_bd_enzyme_N. IPR011766. TPP_enzyme_bd_C. IPR012000. TPP_enzyme_M. [Graphical view] |
| Pfam | PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02418. acolac_catab. 1 hit. |
| PROSITE | PS00187. TPP_ENZYMES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ILVB_KLETE | ||||||||
| Accession | Primary (citable) accession number: Q04524 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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