ILV5_ORYSJ
ID ILV5_ORYSJ Reviewed; 578 AA.
AC Q65XK0; A0A0P0WRB0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ketol-acid reductoisomerase, chloroplastic;
DE EC=1.1.1.86;
DE AltName: Full=Acetohydroxy-acid reductoisomerase;
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
DE AltName: Full=Protein KARI;
DE Flags: Precursor;
GN OrderedLocusNames=Os05g0573700, LOC_Os05g49800; ORFNames=OJ1735_C10.18;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 54-578 IN COMPLEX WITH MAGNESIUM
RP IONS AND NADPH, AND SUBUNIT.
RX PubMed=19362563; DOI=10.1016/j.jmb.2009.04.012;
RA Leung E.W.W., Guddat L.W.;
RT "Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+)
RT and NADPH binding as revealed by two crystal structures.";
RL J. Mol. Biol. 389:167-182(2009).
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per subunit.;
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 from
CC pyruvate: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19362563}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000305}.
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DR EMBL; AC104284; AAU44107.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18298.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS95451.1; -; Genomic_DNA.
DR EMBL; AK065295; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015640421.1; XM_015784935.1.
DR PDB; 3FR7; X-ray; 1.55 A; A/B=54-578.
DR PDB; 3FR8; X-ray; 2.80 A; A/B=54-578.
DR PDBsum; 3FR7; -.
DR PDBsum; 3FR8; -.
DR AlphaFoldDB; Q65XK0; -.
DR SMR; Q65XK0; -.
DR STRING; 4530.OS05T0573700-01; -.
DR ChEMBL; CHEMBL2366499; -.
DR PaxDb; Q65XK0; -.
DR PRIDE; Q65XK0; -.
DR EnsemblPlants; Os05t0573700-01; Os05t0573700-01; Os05g0573700.
DR GeneID; 4339677; -.
DR Gramene; Os05t0573700-01; Os05t0573700-01; Os05g0573700.
DR KEGG; osa:4339677; -.
DR eggNOG; ENOG502QQBF; Eukaryota.
DR InParanoid; Q65XK0; -.
DR OMA; FKNTVEC; -.
DR OrthoDB; 720924at2759; -.
DR BRENDA; 1.1.1.86; 4460.
DR PlantReactome; R-OSA-1119460; Isoleucine biosynthesis from threonine.
DR PlantReactome; R-OSA-1119600; Valine biosynthesis.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR EvolutionaryTrace; Q65XK0; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q65XK0; baseline and differential.
DR Genevisible; Q65XK0; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
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; IPR016206; KetolA_reductoisomerase_plant.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21371; PTHR21371; 1.
DR Pfam; PF01450; IlvC; 2.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000118; Ilv5_plant; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51851; KARI_C; 2.
DR PROSITE; PS51850; KARI_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Chloroplast; Magnesium;
KW Metal-binding; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..578
FT /note="Ketol-acid reductoisomerase, chloroplastic"
FT /id="PRO_0000383458"
FT DOMAIN 90..288
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 289..437
FT /note="KARI C-terminal knotted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT DOMAIN 438..574
FT /note="KARI C-terminal knotted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 208
FT /evidence="ECO:0000255"
FT BINDING 111..118
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19362563"
FT BINDING 144..149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19362563"
FT BINDING 183..187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19362563"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 500
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT CONFLICT 173
FT /note="S -> F (in Ref. 5; AK065295)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="S -> L (in Ref. 5; AK065295)"
FT /evidence="ECO:0000305"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:3FR7"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:3FR7"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:3FR7"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 307..322
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 360..390
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 422..433
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 444..463
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 468..475
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 483..490
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 492..498
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 501..520
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 522..527
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:3FR7"
FT HELIX 545..553
FT /evidence="ECO:0007829|PDB:3FR7"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:3FR8"
SQ SEQUENCE 578 AA; 62377 MW; C81C84F7F03F5506 CRC64;
MAASTTLALS HPKTLAAAAA AAPKAPTAPA AVSFPVSHAA CAPLAARRRA VTAMVAAPPA
VGAAMPSLDF DTSVFNKEKV SLAGHEEYIV RGGRNLFPLL PEAFKGIKQI GVIGWGSQGP
AQAQNLRDSL AEAKSDIVVK IGLRKGSKSF DEARAAGFTE ESGTLGDIWE TVSGSDLVLL
LISDAAQADN YEKIFSHMKP NSILGLSHGF LLGHLQSAGL DFPKNISVIA VCPKGMGPSV
RRLYVQGKEI NGAGINSSFA VHQDVDGRAT DVALGWSVAL GSPFTFATTL EQEYKSDIFG
ERGILLGAVH GIVEALFRRY TEQGMDEEMA YKNTVEGITG IISKTISKKG MLEVYNSLTE
EGKKEFNKAY SASFYPCMDI LYECYEDVAS GSEIRSVVLA GRRFYEKEGL PAFPMGNIDQ
TRMWKVGEKV RSTRPENDLG PLHPFTAGVY VALMMAQIEV LRKKGHSYSE IINESVIESV
DSLNPFMHAR GVAFMVDNCS TTARLGSRKW APRFDYILTQ QAFVTVDKDA PINQDLISNF
MSDPVHGAIE VCAELRPTVD ISVPANADFV RPELRQSS
