Reviewed,
UniProtKB/Swiss-Prot O78518 (ILVB_GUITH)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 |
| ||
| Encoded on | Plastid; Chloroplast | ||
| Organism | Guillardia theta (Cryptomonas phi) | ||
| Taxonomic identifier | 55529 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Cryptophyta › Pyrenomonadales › Geminigeraceae › Guillardia |
Protein attributes
| Sequence length | 575 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. |
| 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. |
| Subcellular location | |
| Sequence similarities | Belongs to the TPP enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis |
| Cellular component | Chloroplast Plastid |
| Ligand | FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate |
| Molecular function | Transferase |
| Gene Ontology (GO) | |
| Biological process | branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – 575 | 575 | Acetolactate synthase large subunit | PRO_0000090810 | |||||
Regions | |||||||||
| Nucleotide binding | 270 – 291 | 22 | FAD By similarity | ||||||
| Nucleotide binding | 313 – 332 | 20 | FAD By similarity | ||||||
| Region | 404 – 483 | 80 | Thiamine pyrophosphate binding | ||||||
Sites | |||||||||
| Metal binding | 454 | 1 | Magnesium By similarity | ||||||
| Metal binding | 481 | 1 | Magnesium By similarity | ||||||
| Binding site | 60 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 162 | 1 | FAD By similarity | ||||||
Sequences
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References
| [1] | "The plastid genome of the cryptophyte alga, Guillardia theta: complete sequence and conserved synteny groups confirm its common ancestry with red algae." Douglas S.E., Penny S.L. J. Mol. Evol. 48:236-244(1999) [PubMed: 9929392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF041468 Genomic DNA. Translation: AAC35740.1. | |
| RefSeq | NP_050806.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JSC based on UniProtKB P07342. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 857117. |
Phylogenomic databases | |
| HOGENOM | O78518. |
| OMA | O78518. HSWRYDH. |
Enzyme and pathway databases | |
| BRENDA | 2.2.1.6. 279957. |
Family and domain databases | |
| InterPro | IPR012846. Acetolactate_synth_lsu. 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 | TIGR00118. acolac_lg. 1 hit. |
| PROSITE | PS00187. TPP_ENZYMES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ILVB_GUITH | ||||||||
| Accession | Primary (citable) accession number: O78518 | ||||||||
| 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 |

Clusters with


