Q1QUR0 (LEU3_CHRSD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 42.
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 |
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| Organism | Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 290398 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Halomonadaceae › Chromohalobacter |
Protein attributes
| Sequence length | 359 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 By similarity. 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. |
| Sequence caution | The sequence ABE59798.1 differs from that shown. Reason: Erroneous initiation. |
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 – 359 | 359 | 3-isopropylmalate dehydrogenase HAMAP MF_01033 | PRO_0000250112 | |||||
Regions | |||||||||
| Nucleotide binding | 281 – 293 | 13 | NAD By similarity | ||||||
Sites | |||||||||
| Metal binding | 223 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 247 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 251 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 96 | 1 | Substrate By similarity | ||||||
| Binding site | 106 | 1 | Substrate By similarity | ||||||
| Binding site | 134 | 1 | Substrate By similarity | ||||||
| Binding site | 223 | 1 | Substrate By similarity | ||||||
| Site | 141 | 1 | Important for catalysis By similarity | ||||||
| Site | 191 | 1 | Important for catalysis By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of Chromohalobacter salexigens DSM 3043." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. Richardson P.Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 3043 / ATCC BAA-138 / NCIMB 13768. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000285 Genomic DNA. Translation: ABE59798.1. Different initiation. |
| RefSeq | YP_574497.1. NC_007963.1. |
3D structure databases | |
| ProteinModelPortal | Q1QUR0. |
| SMR | Q1QUR0. Positions 3-356. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1QUR0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4026971. |
| GenomeReviews | Gene locus Csal_2451 in contig CP000285_GR. |
| KEGG | csa:Csal_2451. |
| NMPDR | fig|290398.4.peg.3092. |
| PATRIC | 21448744. VBIChrSal113723_2460. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0473. |
| HOGENOM | HBG518924. |
Enzyme and pathway databases | |
| BioCyc | CSAL290398:CSAL_2451-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_CHRSD | ||||||||
| Accession | Primary (citable) accession number: Q1QUR0 | ||||||||
| 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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