Q7WNM3 (LEU31_BORBR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
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 1 EC=1.1.1.85 Alternative name(s): 3-IPM-DH 1 Beta-IPM dehydrogenase 1 Short name=IMDH 1 | ||||
| Gene names |
| ||||
| Organism | Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 257310 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 370 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. |
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 – 370 | 370 | 3-isopropylmalate dehydrogenase 1 HAMAP MF_01033 | PRO_0000250103 | |||||
Regions | |||||||||
| Nucleotide binding | 289 – 301 | 13 | NAD By similarity | ||||||
Sites | |||||||||
| Metal binding | 227 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 251 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 255 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 98 | 1 | Substrate By similarity | ||||||
| Binding site | 108 | 1 | Substrate By similarity | ||||||
| Binding site | 136 | 1 | Substrate By similarity | ||||||
| Binding site | 227 | 1 | Substrate By similarity | ||||||
| Site | 143 | 1 | Important for catalysis By similarity | ||||||
| Site | 194 | 1 | Important for catalysis By similarity | ||||||
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-588 / NCTC 13252 / RB50. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640440 Genomic DNA. Translation: CAE31513.1. |
| RefSeq | NP_887562.1. NC_002927.3. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A05 based on UniProtKB Q56268. |
| ProteinModelPortal | Q7WNM3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2663175. |
| GenomeReviews | Gene locus BB1014 in contig BX470250_GR. |
| KEGG | bbr:BB1014. |
| NMPDR | fig|257310.1.peg.1009. |
| PATRIC | 21135262. VBIBorBro124907_1027. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG518924. |
| PhylomeDB | Q7WNM3. |
Enzyme and pathway databases | |
| BioCyc | BBRO257310:BB1014-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 | LEU31_BORBR | ||||||||
| Accession | Primary (citable) accession number: Q7WNM3 | ||||||||
| 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 |

Clusters with