ILV5_YEAST
ID ILV5_YEAST Reviewed; 395 AA.
AC P06168; D6VYZ3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Ketol-acid reductoisomerase, mitochondrial {ECO:0000305};
DE EC=1.1.1.86 {ECO:0000305|PubMed:3027658};
DE AltName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000303|PubMed:3027658};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
DE AltName: Full=Isoleucine-plus-valine requiring protein 5 {ECO:0000303|PubMed:3027658};
DE Flags: Precursor;
GN Name=ILV5 {ECO:0000303|PubMed:3027658}; OrderedLocusNames=YLR355C;
GN ORFNames=L9638.7;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=3027658; DOI=10.1093/nar/14.24.9631;
RA Petersen J.G.L., Holmberg S.;
RT "The ILV5 gene of Saccharomyces cerevisiae is highly expressed.";
RL Nucleic Acids Res. 14:9631-9651(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 166-174.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [5]
RP IDENTIFICATION OF PROBABLE N-TERMINUS.
RX PubMed=8962070; DOI=10.1073/pnas.93.25.14440;
RA Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M.,
RA Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.;
RT "Linking genome and proteome by mass spectrometry: large-scale
RT identification of yeast proteins from two dimensional gels.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids
CC (BCAA). Catalyzes the second common step in the parallel biosynthesis
CC of isoleucine and valine. Converts alpha-aceto-alpha-hydroxybutyrate
CC (AHB) to alpha,beta-dihydroxy-beta-methylvalerate (DHMV) and alpha-
CC acetolactate (AL) to alpha,beta-dihydroxy-isovalerate (DHV) in
CC isoleucine and valine biosynthesis, respectively.
CC {ECO:0000305|PubMed:3027658}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58476; EC=1.1.1.86;
CC Evidence={ECO:0000305|PubMed:3027658};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22070;
CC Evidence={ECO:0000305|PubMed:3027658};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-
CC ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13495;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000305|PubMed:3027658}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000305|PubMed:3027658}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: Present with 883000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000305}.
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DR EMBL; X04969; CAA28643.1; -; Genomic_DNA.
DR EMBL; U19102; AAB67753.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09659.1; -; Genomic_DNA.
DR PIR; A24709; A24709.
DR RefSeq; NP_013459.1; NM_001182244.1.
DR AlphaFoldDB; P06168; -.
DR SMR; P06168; -.
DR BioGRID; 31617; 148.
DR DIP; DIP-6463N; -.
DR IntAct; P06168; 38.
DR MINT; P06168; -.
DR STRING; 4932.YLR355C; -.
DR MoonProt; P06168; -.
DR CarbonylDB; P06168; -.
DR iPTMnet; P06168; -.
DR SWISS-2DPAGE; P06168; -.
DR MaxQB; P06168; -.
DR PaxDb; P06168; -.
DR PRIDE; P06168; -.
DR TopDownProteomics; P06168; -.
DR EnsemblFungi; YLR355C_mRNA; YLR355C; YLR355C.
DR GeneID; 851069; -.
DR KEGG; sce:YLR355C; -.
DR SGD; S000004347; ILV5.
DR VEuPathDB; FungiDB:YLR355C; -.
DR eggNOG; ENOG502QQBF; Eukaryota.
DR HOGENOM; CLU_033821_1_2_1; -.
DR InParanoid; P06168; -.
DR OMA; RAMFSWL; -.
DR BioCyc; YEAST:YLR355C-MON; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR PRO; PR:P06168; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P06168; protein.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IMP:SGD.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 3.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013023; KARI.
DR InterPro; IPR000506; KARI_C.
DR InterPro; IPR013116; KARI_N.
DR InterPro; IPR016207; KetolA_reductoisomerase_fun.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00465; ilvC; 1.
DR PROSITE; PS51851; KARI_C; 1.
DR PROSITE; PS51850; KARI_N; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Direct protein sequencing; Magnesium; Metal-binding; Mitochondrion; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..395
FT /note="Ketol-acid reductoisomerase, mitochondrial"
FT /id="PRO_0000015634"
FT DOMAIN 57..246
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 247..394
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT REGION 363..395
FT /note="Hydrophilic"
FT ACT_SITE 171
FT /evidence="ECO:0000255"
FT BINDING 84..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 108..113
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 146..150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 395 AA; 44368 MW; D76419A6AD68E85E CRC64;
MLRTQAARLI CNSRVITAKR TFALATRAAA YSRPAARFVK PMITTRGLKQ INFGGTVETV
YERADWPREK LLDYFKNDTF ALIGYGSQGY GQGLNLRDNG LNVIIGVRKD GASWKAAIED
GWVPGKNLFT VEDAIKRGSY VMNLLSDAAQ SETWPAIKPL LTKGKTLYFS HGFSPVFKDL
THVEPPKDLD VILVAPKGSG RTVRSLFKEG RGINSSYAVW NDVTGKAHEK AQALAVAIGS
GYVYQTTFER EVNSDLYGER GCLMGGIHGM FLAQYDVLRE NGHSPSEAFN ETVEEATQSL
YPLIGKYGMD YMYDACSTTA RRGALDWYPI FKNALKPVFQ DLYESTKNGT ETKRSLEFNS
QPDYREKLEK ELDTIRNMEI WKVGKEVRKL RPENQ
