Q9WYC7 (LEUC1_THEMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 77.
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 1 EC=4.2.1.33 Alternative name(s): Alpha-IPM isomerase 1 Short name=IPMI 1 Isopropylmalate isomerase 1 | ||||
| Gene names |
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| Organism | Thermotoga maritima | ||||
| Taxonomic identifier | 2336 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga |
Protein attributes
| Sequence length | 418 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. HAMAP MF_01027 |
| Catalytic activity | (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O. HAMAP MF_01027 (2S)-2-isopropylmaleate + H2O = (2S)-2-isopropylmalate. HAMAP MF_01027 |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP MF_01027 |
| Pathway | Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP MF_01027 |
| Subunit structure | Heterodimer of LeuC and LeuD By similarity. HAMAP MF_01027 |
| Sequence similarities | Belongs to the aconitase/IPM isomerase family. LeuC type 2 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | leucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: EC 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 – 418 | 418 | 3-isopropylmalate dehydratase large subunit 1 HAMAP MF_01027 | PRO_0000076860 | |||||
Sites | |||||||||
| Metal binding | 298 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 358 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 361 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| [1] | "Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M.Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000512 Genomic DNA. Translation: AAD35379.1. |
| PIR | C72394. |
| RefSeq | NP_228103.1. NC_000853.1. |
3D structure databases | |
| ProteinModelPortal | Q9WYC7. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 897215. |
| GenomeReviews | Gene locus TM_0291 in contig AE000512_GR. |
| KEGG | tma:TM0291. |
| NMPDR | fig|243274.1.peg.287. |
| PATRIC | 23935461. VBITheMar51294_0296. |
| TIGR | TM_0291. |
Phylogenomic databases | |
| HOGENOM | HBG330745. |
| OMA | KGEISDP. |
| PhylomeDB | Q9WYC7. |
| ProtClustDB | PRK00402. |
Enzyme and pathway databases | |
| BioCyc | TMAR243274:TM_0291-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01027. LeuC_type2. [Tree] |
| InterPro | 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. IPR011826. HAcnase/IPMdehydase_lsu_prok. IPR006251. Homoacnase/IPMdehydase_lsu. [Graphical view] |
| Gene3D | G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit. |
| KO | K01703. |
| PANTHER | PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF16. PTHR11670:SF16. 1 hit. |
| Pfam | PF00330. Aconitase. 2 hits. [Graphical view] |
| PRINTS | PR00415. ACONITASE. |
| SUPFAM | SSF53732. Aconitase_N. 1 hit. |
| TIGRFAMs | TIGR01343. HacA_fam. 1 hit. TIGR02086. IPMI_arch. 1 hit. |
| PROSITE | PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LEUC1_THEMA | ||||||||
| Accession | Primary (citable) accession number: Q9WYC7 | ||||||||
| 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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