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Database: UniProt/SWISS-PROT
Entry: ILV5_SCHPO
LinkDB: ILV5_SCHPO
Original site: ILV5_SCHPO 
ID   ILV5_SCHPO              Reviewed;         404 AA.
AC   P78827; O42619;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   11-JUN-2014, entry version 114.
DE   RecName: Full=Probable ketol-acid reductoisomerase, mitochondrial;
DE            EC=1.1.1.86;
DE   AltName: Full=Acetohydroxy-acid reductoisomerase;
DE   AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
DE   Flags: Precursor;
GN   Name=ilv5; ORFNames=SPBC56F2.12;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 262-404.
RA   Kawamukai M.;
RT   "S.pombe ILV5 homolog.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
CC       = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CC   -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
CC       NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 2/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
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DR   EMBL; D89175; BAA13837.1; -; mRNA.
DR   EMBL; CU329671; CAA18891.1; -; Genomic_DNA.
DR   EMBL; AB009603; BAA24000.1; -; mRNA.
DR   PIR; T40532; T40532.
DR   RefSeq; NP_001018845.2; NM_001022630.3.
DR   ProteinModelPortal; P78827; -.
DR   BioGrid; 280430; 4.
DR   MINT; MINT-4691399; -.
DR   STRING; 4896.SPBC56F2.12-1; -.
DR   MaxQB; P78827; -.
DR   PaxDb; P78827; -.
DR   EnsemblFungi; SPBC56F2.12.1; SPBC56F2.12.1:pep; SPBC56F2.12.
DR   GeneID; 3361354; -.
DR   KEGG; spo:SPBC56F2.12; -.
DR   PomBase; SPBC56F2.12; -.
DR   eggNOG; COG0059; -.
DR   HOGENOM; HOG000016231; -.
DR   KO; K00053; -.
DR   OMA; YKTTFEK; -.
DR   OrthoDB; EOG7VHT6S; -.
DR   PhylomeDB; P78827; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   NextBio; 20811414; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; ISS:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; ISS:PomBase.
DR   GO; GO:0006551; P:leucine metabolic process; ISS:PomBase.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; ISS:PomBase.
DR   GO; GO:0009099; P:valine biosynthetic process; ISS:PomBase.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013023; AcH_isomrdctse.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR013116; IlvN.
DR   InterPro; IPR016207; KetolA_reductoisomerase_fun.
DR   PANTHER; PTHR21371; PTHR21371; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000119; Ilv5_fungal; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; Mitochondrion; NADP;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    404       Probable ketol-acid reductoisomerase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000015633.
FT   NP_BIND      91    100       NADP (Potential).
FT   NP_BIND     115    120       NADP (By similarity).
FT   NP_BIND     153    157       NADP (By similarity).
FT   ACT_SITE    178    178       Potential.
FT   METAL       262    262       Magnesium 1 (By similarity).
FT   METAL       262    262       Magnesium 2 (By similarity).
FT   METAL       266    266       Magnesium 1 (By similarity).
FT   MOD_RES     261    261       Phosphoserine.
FT   CONFLICT     38     38       S -> R (in Ref. 1; BAA13837).
FT   CONFLICT     92     92       Y -> S (in Ref. 1; BAA13837).
FT   CONFLICT    275    275       N -> P (in Ref. 1; BAA13837).
FT   CONFLICT    297    297       N -> P (in Ref. 1; BAA13837).
FT   CONFLICT    394    394       V -> G (in Ref. 1; BAA13837).
SQ   SEQUENCE   404 AA;  45189 MW;  9AB3674C71AD6FEB CRC64;
     MSFRNSSRMA MKALRTMGSR RLATRSMSVM ARTIAAPSMR FAPRMTAPLM QTRGMRVMDF
     AGTKENVWER SDWPREKLVD YFKNDTLAII GYGSQGHGQG LNARDQGLNV IVGVRKDGAS
     WKQAIEDGWV PGKTLFPVEE AIKKGSIIMN LLSDAAQTET WPKIAPLITK GKTLYFSHGF
     SVIFKDQTKI HPPKDVDVIL VAPKGSGRTV RTLFKEGRGI NSSFAVYQDV TGKAQEKAIG
     LAVAVGSGFI YQTTFKKEVI SDLVGERGCL MGGINGLFLA QYQVLRERGH SPAEAFNETV
     EEATQSLYPL IGKYGLDYMF AACSTTARRG AIDWTPRFLE ANKKVLNELY DNVENGNEAK
     RSLEYNSAPN YRELYDKELE EIRNLEIWKA GEVVRSLRPE HNKH
//
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