P65149 (ILVC_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 51.
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: Ketol-acid reductoisomerase EC=1.1.1.86 Alternative name(s): Acetohydroxy-acid isomeroreductase Alpha-keto-beta-hydroxylacil reductoisomerase | ||||||
| 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 | 333 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | (R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. HAMAP MF_00435 (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. HAMAP MF_00435 |
| Pathway | Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. HAMAP MF_00435 Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. HAMAP MF_00435 |
| Sequence similarities | Belongs to the ketol-acid reductoisomerase family. |
| Sequence caution | The sequence AAK47410.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| 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 | cytosol Inferred from direct assay. Source: MTBBASE plasma membraneInferred from direct assay. Source: MTBBASE |
| Molecular function | coenzyme binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 333 | 333 | Ketol-acid reductoisomerase HAMAP MF_00435 | PRO_0000151329 | |||||
Sites | |||||||||
| Active site | 105 | 1 | 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 | BX842581 Genomic DNA. Translation: CAA16086.1. AE000516 Genomic DNA. Translation: AAK47410.1. Different initiation. |
| PIR | D70855. |
| RefSeq | NP_337596.1. NC_002755.2. |
3D structure databases | |
| ProteinModelPortal | P65149. |
| SMR | P65149. Positions 1-325. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000003191; EBMYCP00000003191; EBMYCG00000003189. EBMYCT00000069934; EBMYCP00000067993; EBMYCG00000069929. |
| GeneID | 926692. |
| GenomeReviews | Gene locus MT3081 in contig AE000516_GR. Gene locus Rv3001c in contig AL123456_GR. |
| KEGG | mtc:MT3081. mtu:Rv3001c. |
| PATRIC | 18128542. VBIMycTub22151_3369. |
| TIGR | MT3081. |
Organism-specific databases | |
| TubercuList | Rv3001c. |
Phylogenomic databases | |
| GeneTree | EBGT00050000015910. |
| HOGENOM | HBG286525. |
| OMA | EYANGRG. |
| PhylomeDB | P65149. |
| ProtClustDB | PRK05479. |
Family and domain databases | |
| HAMAP | MF_00435. IlvC. [Tree] |
| InterPro | IPR008927. 6-PGluconate_DH_C-like. IPR013023. AcH_isomrdctse. IPR000506. AcH_isomrdctse_C. IPR013328. DH_multihelical. IPR013116. IlvN. [Graphical view] |
| Gene3D | G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| KO | K00053. |
| PANTHER | PTHR21371. AcH_isomrdctse. 1 hit. |
| Pfam | PF01450. IlvC. 1 hit. PF07991. IlvN. 1 hit. [Graphical view] |
| SUPFAM | SSF48179. 6DGDH_C_like. 1 hit. |
| TIGRFAMs | TIGR00465. IlvC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ILVC_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65149 Secondary accession number(s): O53248 | ||||||||
| 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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