P87257 (LEU3B_ASPNG) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 72.
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 B Short name=3-IPM-DH B Short name=IMDH B EC=1.1.1.85 Alternative name(s): Beta-IPM dehydrogenase B | ||
| Gene names |
| ||
| Organism | Aspergillus niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 371 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
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. |
| Catalytic activity | (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. |
| 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. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the isocitrate and isopropylmalate dehydrogenases family. |
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 |
| 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 – 371 | 371 | 3-isopropylmalate dehydrogenase B | PRO_0000083600 | |||||
Regions | |||||||||
| Nucleotide binding | 79 – 93 | 15 | NAD By similarity | ||||||
| Nucleotide binding | 296 – 308 | 13 | NAD By similarity | ||||||
Sites | |||||||||
| Metal binding | 229 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 254 | 1 | Magnesium or manganese By similarity | ||||||
| Metal binding | 258 | 1 | Magnesium or manganese By similarity | ||||||
| Binding site | 100 | 1 | Substrate By similarity | ||||||
| Binding site | 110 | 1 | Substrate By similarity | ||||||
| Binding site | 142 | 1 | Substrate By similarity | ||||||
| Binding site | 229 | 1 | Substrate By similarity | ||||||
| Site | 149 | 1 | Important for catalysis By similarity | ||||||
| Site | 196 | 1 | Important for catalysis By similarity | ||||||
Sequences
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References
| [1] | "Isolation by genetic complementation of two differentially expressed genes for beta-isopropylmalate dehydrogenase from Aspergillus niger." Williams B.A., Sillaots S., Tsang A., Storms R. Curr. Genet. 30:305-311(1996) [PubMed: 8781173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: A733. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | S83229 mRNA. Translation: AAB50828.1. U51131 mRNA. Translation: AAD10279.1. |
| PIR | S72210. |
3D structure databases | |
| ProteinModelPortal | P87257. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P87257. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| 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. |
| 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 | LEU3B_ASPNG | ||||||||
| Accession | Primary (citable) accession number: P87257 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with