O33112 (ILVB_MYCLE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
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: Acetolactate synthase EC=2.2.1.6 Alternative name(s): ALS Acetohydroxy-acid synthase | ||||||
| Gene names |
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| Organism | Mycobacterium leprae [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1769 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 625 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 2 pyruvate = 2-acetolactate + CO2. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity. |
| Pathway | Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. |
| Sequence similarities | Belongs to the TPP enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis |
| Ligand | FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | acetolactate synthase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro magnesium ion bindingInferred from electronic annotation. Source: InterPro thiamine 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 – 625 | 625 | Acetolactate synthase | PRO_0000090802 | |||||
Regions | |||||||||
| Nucleotide binding | 300 – 321 | 22 | FAD By similarity | ||||||
| Nucleotide binding | 343 – 362 | 20 | FAD By similarity | ||||||
| Region | 436 – 516 | 81 | Thiamine pyrophosphate binding | ||||||
Sites | |||||||||
| Metal binding | 487 | 1 | Magnesium By similarity | ||||||
| Metal binding | 514 | 1 | Magnesium By similarity | ||||||
| Binding site | 92 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 194 | 1 | FAD By similarity | ||||||
Sequences
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References
| [1] | "Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G.Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z99263 Genomic DNA. Translation: CAB16435.1. AL583923 Genomic DNA. Translation: CAC30649.1. |
| PIR | T45413. |
| RefSeq | NP_302166.1. NC_002677.1. |
3D structure databases | |
| ProteinModelPortal | O33112. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000029089; EBMYCP00000028695; EBMYCG00000029084. |
| GeneID | 910798. |
| GenomeReviews | Gene locus ML1696 in contig AL450380_GR. |
| KEGG | mle:ML1696. |
| NMPDR | fig|272631.1.peg.1038. |
| PATRIC | 18056540. VBIMycLep78757_3199. |
Organism-specific databases | |
| Leproma | ML1696. |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000014643. |
| HOGENOM | HBG323037. |
| OMA | RLVFIDI. |
| ProtClustDB | PRK07789. |
Enzyme and pathway databases | |
| BioCyc | MLEP272631:ML1696-MONOMER. |
Family and domain databases | |
| InterPro | IPR012846. Acetolactate_synth_lsu. IPR012000. Thiamin_PyroP_enz_cen_dom. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. IPR000399. TPP-bd_CS. IPR011766. TPP_enzyme-bd_C. [Graphical view] |
| KO | K01652. |
| PANTHER | PTHR18968:SF13. PTHR18968:SF13. 1 hit. |
| Pfam | PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00118. Acolac_lg. 1 hit. |
| PROSITE | PS00187. TPP_ENZYMES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ILVB_MYCLE | ||||||||
| Accession | Primary (citable) accession number: O33112 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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