P45261 (ILVI_HAEIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 88.
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 large subunit Short name=AHAS EC=2.2.1.6 Alternative name(s): Acetohydroxy-acid synthase large subunit Short name=ALS | ||||
| Gene names |
| ||||
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) | ||||
| Taxonomic identifier | 71421 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 573 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. |
| Subunit structure | Dimer of large and small chains By similarity. |
| Miscellaneous | Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry By similarity. |
| 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 Reference 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 – 573 | 573 | Acetolactate synthase large subunit | PRO_0000090795 | |||||
Regions | |||||||||
| Nucleotide binding | 261 – 282 | 22 | FAD By similarity | ||||||
| Nucleotide binding | 304 – 323 | 20 | FAD By similarity | ||||||
| Region | 396 – 476 | 81 | Thiamine pyrophosphate binding | ||||||
Sites | |||||||||
| Metal binding | 447 | 1 | Magnesium By similarity | ||||||
| Metal binding | 474 | 1 | Magnesium By similarity | ||||||
| Binding site | 51 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 153 | 1 | FAD By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L42023 Genomic DNA. Translation: AAC23233.1. |
| PIR | C64131. |
| RefSeq | NP_439730.1. NC_000907.1. |
3D structure databases | |
| ProteinModelPortal | P45261. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 950449. |
| GenomeReviews | Gene locus HI_1585 in contig L42023_GR. |
| KEGG | hin:HI1585. |
| NMPDR | fig|71421.1.peg.1505. |
| PATRIC | 20191903. VBIHaeInf48452_1659. |
| TIGR | HI_1585. |
Phylogenomic databases | |
| HOGENOM | HBG323037. |
| OMA | RLVFIDI. |
| PhylomeDB | P45261. |
| ProtClustDB | PRK06882. |
Enzyme and pathway databases | |
| BioCyc | HINF71421:HI_1585-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 | ILVI_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P45261 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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