Reviewed,
UniProtKB/Swiss-Prot P42463 (ILVB_CORGL)
Last modified
June 16, 2009.
Version 69.
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 |
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| Organism | Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1718 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 626 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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. |
| 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 |
| Gene Ontology (GO) | |
| Biological process | branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 626 | 626 | Acetolactate synthase large subunit | PRO_0000090787 | |||||
Regions | |||||||||
| Nucleotide binding | 281 – 302 | 22 | FAD By similarity | ||||||
| Nucleotide binding | 324 – 343 | 20 | FAD By similarity | ||||||
| Region | 416 – 496 | 81 | Thiamine pyrophosphate binding | ||||||
Sites | |||||||||
| Metal binding | 467 | 1 | Magnesium By similarity | ||||||
| Metal binding | 494 | 1 | Magnesium By similarity | ||||||
| Binding site | 73 | 1 | Thiamine pyrophosphate By similarity | ||||||
| Binding site | 175 | 1 | FAD By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon." Keilhauer C., Eggeling L., Sahm H. J. Bacteriol. 175:5595-5603(1993) [PubMed: 8366043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [2] | "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [3] | "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A.J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
Cross-references
Sequence databases | |
|---|---|
| L09232 Genomic DNA. Translation: AAA62429.1. BA000036 Genomic DNA. Translation: BAB98664.1. BX927151 Genomic DNA. Translation: CAF19974.1. | |
| PIR | A48648. |
| RefSeq | NP_600493.1. YP_225560.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N0H based on UniProtKB P07342. |
| ModBase | Search... |
2-D gel databases | |
| World-2DPAGE | 0001:P42463. |
Proteomic databases | |
| PRIDE | P42463. |
Genome annotation databases | |
| GeneID | 1019252. 3345149. |
| GenomeReviews | Gene locus Cgl1271 in contig BA000036_GR. Gene locus cg1435 in contig BX927147_GR. |
| KEGG | cgb:cg1435. cgl:NCgl1222. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P42463. |
| OMA | P42463. DIPRIVH. |
Enzyme and pathway databases | |
| BioCyc | CGLU196627-1:CG1435-MON. |
| BRENDA | 2.2.1.6. 812. |
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_CORGL | ||||||||
| Accession | Primary (citable) accession number: P42463 | ||||||||
| 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


