Q6HLF2 (LEU3_BACHK) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 57.
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: 3-isopropylmalate dehydrogenase EC=1.1.1.85 Alternative name(s): 3-IPM-DH Beta-IPM dehydrogenase Short name=IMDH | ||||
| Gene names |
| ||||
| Organism | Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 281309 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. HAMAP MF_01033 |
| Catalytic activity | (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. HAMAP MF_01033 |
| Cofactor | Binds 1 magnesium or manganese ion per subunit By similarity. |
| Pathway | Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. HAMAP MF_01033 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01033 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01033. |
| Sequence similarities | Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Manganese Metal-binding NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | leucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3-isopropylmalate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD bindingInferred from electronic annotation. Source: InterPro magnesium ion 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 – 354 | 354 | 3-isopropylmalate dehydrogenase HAMAP MF_01033 | PRO_0000083643 | |||||
Regions | |||||||||
| Nucleotide binding | 76 – 87 | 12 | NAD By similarity | ||||||
| Nucleotide binding | 273 – 285 | 13 | NAD By similarity | ||||||
Sites | |||||||||
| Metal binding | 215 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 239 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 243 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 94 | 1 | Substrate By similarity | ||||||
| Binding site | 104 | 1 | Substrate By similarity | ||||||
| Binding site | 130 | 1 | Substrate By similarity | ||||||
| Binding site | 215 | 1 | Substrate By similarity | ||||||
| Site | 137 | 1 | Important for catalysis By similarity | ||||||
| Site | 183 | 1 | Important for catalysis By similarity | ||||||
Sequences
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References
| [1] | "Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. Gilna P.J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017355 Genomic DNA. Translation: AAT59415.1. |
| RefSeq | YP_035619.1. NC_005957.1. |
3D structure databases | |
| ProteinModelPortal | Q6HLF2. |
| SMR | Q6HLF2. Positions 1-344. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000072437; EBBACP00000070523; EBBACG00000072428. |
| GeneID | 2855825. |
| GenomeReviews | Gene locus BT9727_1285 in contig AE017355_GR. |
| KEGG | btk:BT9727_1285. |
| NMPDR | fig|281309.1.peg.1259. |
| PATRIC | 18983249. VBIBacThu119411_1354. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000000661. |
| HOGENOM | HBG518924. |
| OMA | LDKNNKG. |
| ProtClustDB | PRK00772. |
Enzyme and pathway databases | |
| BioCyc | BTHU281309:BT9727_1285-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01033. LeuB_type1. [Tree] |
| InterPro | IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR024084. IsoPropMal-DH-like_dom. IPR004429. Isopropylmalate_DH. [Graphical view] |
| Gene3D | G3DSA:3.40.718.10. IDH_IMDH. 1 hit. |
| KO | K00052. |
| PANTHER | PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF13. IPMDH. 1 hit. |
| Pfam | PF00180. Iso_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00169. LeuB. 1 hit. |
| PROSITE | PS00470. IDH_IMDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LEU3_BACHK | ||||||||
| Accession | Primary (citable) accession number: Q6HLF2 | ||||||||
| 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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