Reviewed,
UniProtKB/Swiss-Prot P78827 (ILV5_SCHPO)
Last modified
November 25, 2008.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Probable ketol-acid reductoisomerase, mitochondrial EC=1.1.1.86 Alternative name(s): Acetohydroxy-acid reductoisomerase Alpha-keto-beta-hydroxylacil reductoisomerase | ||||
| Gene names |
| ||||
| Organism | Schizosaccharomyces pombe (Fission yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4896 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces |
Protein attributes
| Sequence length | 404 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. |
| Pathway | Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. |
| Subcellular location | MitochondrionBy similarity. |
| Sequence similarities | Belongs to the ketol-acid reductoisomerase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | coenzyme binding Inferred from electronic annotation. Source: InterPro ketol-acid reductoisomerase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 404 | Probable ketol-acid reductoisomerase, mitochondrial | PRO_0000015633 | ||||||
Sites | |||||||||
| Active site | 178 | 1 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 261 | 1 | Phosphoserine | ||||||
Experimental info | |||||||||
| Sequence conflict | 38 | 1 | S → R in BAA13837. Ref.1 | ||||||
| Sequence conflict | 92 | 1 | Y → S in BAA13837. Ref.1 | ||||||
| Sequence conflict | 275 | 1 | N → P in BAA13837. Ref.1 | ||||||
| Sequence conflict | 297 | 1 | N → P in BAA13837. Ref.1 | ||||||
| Sequence conflict | 394 | 1 | V → G in BAA13837. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: PR745. |
| [2] | "The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. Nurse P.Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972. |
| [3] | "S.pombe ILV5 homolog." Kawamukai M. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 262-404. |
| [4] | "Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| D89175 mRNA. Translation: BAA13837.1. CU329671 Genomic DNA. Translation: CAA18891.1. AB009603 mRNA. Translation: BAA24000.1. | |
| PIR | T40532. |
| RefSeq | NP_001018845.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NP3 based on UniProtKB Q9HVA2. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3361354. |
| KEGG | spo:SPBC56F2.12. |
Organism-specific databases | |
| GeneDB_Spombe | SPBC56F2.12. |
Enzyme and pathway databases | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-004692-MON. |
Gene expression databases | |
| ArrayExpress | P78827. |
Family and domain databases | |
| InterPro | IPR013023. AcH_isomrdctse. IPR000506. AcH_isomrdctse_C. IPR013328. DHase_multihelical. IPR013116. IlvN. IPR016207. KetolA_reductoisomerase_fun. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| PANTHER | PTHR21371. AcH_isomrdctse. 1 hit. |
| Pfam | PF01450. IlvC. 1 hit. PF07991. IlvN. 1 hit. [Graphical view] |
| PIRSF | PIRSF000119. Ilv5_fungal. 1 hit. |
| TIGRFAMs | TIGR00465. ilvC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ILV5_SCHPO | ||||||||
| Accession | Primary (citable) accession number: P78827 Secondary accession number(s): O42619 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


