Reviewed,
UniProtKB/Swiss-Prot Q5KPJ5 (ILVB_CRYNE)
Last modified
June 16, 2009.
Version 32.
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, mitochondrial EC=2.2.1.6 Alternative name(s): Acetohydroxy-acid synthase ALS AHAS | ||||
| Gene names |
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| Organism | Cryptococcus neoformans (Filobasidiella neoformans) [Complete proteome] | ||||
| Taxonomic identifier | 5207 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex |
Protein attributes
| Sequence length | 718 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. |
| Subcellular location | Mitochondrion By similarity. |
| Sequence similarities | Belongs to the TPP enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| 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 |
| Cellular component | mitochondrion 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 718 | Acetolactate synthase, mitochondrial | PRO_0000035661 | ||||||
Regions | |||||||||
| Nucleotide binding | 397 – 418 | 22 | FAD By similarity | ||||||
| Nucleotide binding | 449 – 468 | 20 | FAD By similarity | ||||||
| Region | 541 – 621 | 81 | Thiamine pyrophosphate binding | ||||||
Sites | |||||||||
| Metal binding | 592 | 1 | Magnesium By similarity | ||||||
| Metal binding | 619 | 1 | Magnesium By similarity | ||||||
| Binding site | 173 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 275 | 1 | FAD By similarity | ||||||
Sequences
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References
| [1] | "The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans." Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S. Hyman R.W.Science 307:1321-1324(2005) [PubMed: 15653466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JEC21. |
Cross-references
Sequence databases | |
|---|---|
| AE017341 Genomic DNA. Translation: AAW40825.1. | |
| RefSeq | XP_566644.1. |
| UniGene | Fne.7718 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3253594. |
| GenomeReviews | Gene locus CNA02570 in contig AE017341_GR. |
| KEGG | cne:CNA02570. |
Phylogenomic databases | |
| HOGENOM | Q5KPJ5. |
| OMA | Q5KPJ5. QGLGAFD. |
Enzyme and pathway databases | |
| BRENDA | 2.2.1.6. 2772. |
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_CRYNE | ||||||||
| Accession | Primary (citable) accession number: Q5KPJ5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


