P65154 (ILVD_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 45.
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: Dihydroxy-acid dehydratase Short name=DAD EC=4.2.1.9 | ||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 575 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O. HAMAP MF_00012 |
| Cofactor | Binds 1 4Fe-4S cluster Potential. |
| Pathway | Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. HAMAP MF_00012 Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. HAMAP MF_00012 |
| Sequence similarities | Belongs to the IlvD/Edd family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW growthInferred from mutant phenotype. Source: MTBBASE |
| Cellular component | plasma membrane Inferred from direct assay. Source: MTBBASE |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW dihydroxy-acid dehydratase activityInferred from electronic annotation. Source: EC 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 – 575 | 575 | Dihydroxy-acid dehydratase HAMAP MF_00012 | PRO_0000103481 | |||||
Sites | |||||||||
| Metal binding | 137 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 214 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842572 Genomic DNA. Translation: CAB09740.1. AE000516 Genomic DNA. Translation: AAK44419.1. |
| PIR | H70906. |
| RefSeq | NP_214703.1. NC_000962.2. NP_334605.1. NC_002755.2. |
3D structure databases | |
| ProteinModelPortal | P65154. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000002913; EBMYCP00000002913; EBMYCG00000002911. EBMYCT00000070841; EBMYCP00000068900; EBMYCG00000070836. |
| GeneID | 886774. 923084. |
| GenomeReviews | Gene locus MT0199 in contig AE000516_GR. Gene locus Rv0189c in contig AL123456_GR. |
| KEGG | mtc:MT0199. mtu:Rv0189c. |
| PATRIC | 18122163. VBIMycTub22151_0216. |
| TIGR | MT0199. |
Organism-specific databases | |
| TubercuList | Rv0189c. |
Phylogenomic databases | |
| GeneTree | EBGT00050000016366. |
| HOGENOM | HBG671001. |
| OMA | NMPGAMI. |
| PhylomeDB | P65154. |
| ProtClustDB | PRK00911. |
Family and domain databases | |
| HAMAP | MF_00012. IlvD. [Tree] |
| InterPro | IPR015928. Aconitase/3IPM_dehydase_swvl. IPR004404. DihydroxyA_deHydtase. IPR000581. DiOHA_6PGluconate_deHydtase. IPR020558. DiOHA_6PGluconate_deHydtase_CS. [Graphical view] |
| KO | K01687. |
| PANTHER | PTHR21000. ILVD_EDD_family. 1 hit. |
| Pfam | PF00920. ILVD_EDD. 1 hit. [Graphical view] |
| SUPFAM | SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. |
| TIGRFAMs | TIGR00110. IlvD. 1 hit. |
| PROSITE | PS00886. ILVD_EDD_1. 1 hit. PS00887. ILVD_EDD_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ILVD_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65154 Secondary accession number(s): O07433 | ||||||||
| 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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