B7MNT0 (LEUC_ECO81) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 36.
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 dehydratase large subunit EC=4.2.1.33 Alternative name(s): Alpha-IPM isomerase Short name=IPMI Isopropylmalate isomerase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O81 (strain ED1a) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 585397 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. HAMAP-Rule MF_01026 |
| Catalytic activity | (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01026 |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP-Rule MF_01026 |
| Pathway | Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01026 |
| Subunit structure | Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01026 |
| Sequence similarities | Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | 3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP 4 iron, 4 sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 466 | 466 | 3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026 | PRO_1000149363 | |||||
Sites | |||||||||
| Metal binding | 347 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 407 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 410 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| [1] | "Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. Denamur E.PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ED1a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU928162 Genomic DNA. Translation: CAR06295.1. |
| RefSeq | YP_002396161.1. NC_011745.1. |
3D structure databases | |
| ProteinModelPortal | B7MNT0. |
| SMR | B7MNT0. Positions 4-457. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 585397.ECED1_0072. |
Proteomic databases | |
| PRIDE | B7MNT0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAR06295; CAR06295; ECED1_0072. |
| GeneID | 7141878. |
| KEGG | ecq:ECED1_0072. |
| PATRIC | 38484067. VBIEscCol8292_0077. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0065. |
| HOGENOM | HOG000226972. |
| KO | K01703. |
| OMA | DIRQGIV. |
| ProtClustDB | PRK05478. |
Enzyme and pathway databases | |
| BioCyc | ECOL585397:GJCU-75-MONOMER. |
| UniPathway | UPA00048; UER00071. |
Family and domain databases | |
| Gene3D | 3.30.499.10. 2 hits. 3.40.1060.10. 1 hit. |
| HAMAP | MF_01026. LeuC_type1. |
| InterPro | IPR004430. 3-IsopropMal_deHydase_lsu. IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. [Graphical view] |
| PANTHER | PTHR11670. PTHR11670. 1 hit. |
| Pfam | PF00330. Aconitase. 1 hit. [Graphical view] |
| PRINTS | PR00415. ACONITASE. |
| SUPFAM | SSF53732. Aconitase_N. 1 hit. |
| TIGRFAMs | TIGR00170. leuC. 1 hit. |
| PROSITE | PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LEUC_ECO81 | ||||||||
| Accession | Primary (citable) accession number: B7MNT0 | ||||||||
| 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
