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 01-MAY-2013, entry version 105.
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 MASS
RP 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 STRING; 4896.SPBC56F2.12-1; -.
DR PaxDb; P78827; -.
DR PRIDE; 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; NGMDWMY; -.
DR OrthoDB; EOG4DFSX2; -.
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 PANTHER; PTHR21371:SF3; PTHR21371:SF3; 1.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000119; Ilv5_fungal; 1.
DR SUPFAM; SSF48179; 6DGDH_C_like; 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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