ILV5_SPIOL
ID ILV5_SPIOL Reviewed; 595 AA.
AC Q01292;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Flags: Precursor;
GN Name=AHRI;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-88, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Leaf;
RX PubMed=1713446; DOI=10.1042/bj2770469;
RA Dumas R., Lebrun M., Douce R.;
RT "Isolation, characterization and sequence analysis of a full-length cDNA
RT clone encoding acetohydroxy acid reductoisomerase from spinach
RT chloroplasts.";
RL Biochem. J. 277:469-475(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 72-595 IN COMPLEX WITH NADPH AND
RP MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=9218783; DOI=10.1093/emboj/16.12.3405;
RA Biou V., Dumas R., Cohen-Addad C., Douce R., Job D., Pebay-Peyroula E.;
RT "The crystal structure of plant acetohydroxy acid isomeroreductase
RT complexed with NADPH, two magnesium ions and a herbicidal transition state
RT analog determined at 1.65-A resolution.";
RL EMBO J. 16:3405-3415(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 72-595 IN COMPLEX WITH NADPH AND
RP MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=10739911; DOI=10.1107/s0907444900001694;
RA Thomazeau K., Dumas R., Halgand F., Forest E., Douce R., Biou V.;
RT "Structure of spinach acetohydroxyacid isomeroreductase complexed with its
RT reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-
RT ribose.";
RL Acta Crystallogr. D 56:389-397(2000).
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:10739911,
CC ECO:0000269|PubMed:9218783}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:1713446}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000305}.
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DR EMBL; X57073; CAA40356.1; -; mRNA.
DR PIR; S17180; S17180.
DR PDB; 1QMG; X-ray; 1.60 A; A/B/C/D=72-595.
DR PDB; 1YVE; X-ray; 1.65 A; I/J/K/L=72-595.
DR PDBsum; 1QMG; -.
DR PDBsum; 1YVE; -.
DR AlphaFoldDB; Q01292; -.
DR SMR; Q01292; -.
DR BRENDA; 1.1.1.86; 5812.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR EvolutionaryTrace; Q01292; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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;
KW Direct protein sequencing; Magnesium; Metal-binding; NADP; Oxidoreductase;
KW Plastid; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1713446"
FT CHAIN 73..595
FT /note="Ketol-acid reductoisomerase, chloroplastic"
FT /id="PRO_0000015631"
FT DOMAIN 108..306
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 307..455
FT /note="KARI C-terminal knotted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT DOMAIN 456..592
FT /note="KARI C-terminal knotted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 226
FT /evidence="ECO:0000255"
FT BINDING 129..136
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10739911,
FT ECO:0000269|PubMed:9218783"
FT BINDING 162..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10739911,
FT ECO:0000269|PubMed:9218783"
FT BINDING 201..205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10739911,
FT ECO:0000269|PubMed:9218783"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1QMG"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 244..253
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:1QMG"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:1QMG"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 378..408
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 410..420
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 462..482
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 486..493
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 495..499
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 502..514
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 519..538
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 540..545
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 552..560
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 563..571
FT /evidence="ECO:0007829|PDB:1QMG"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:1QMG"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:1QMG"
SQ SEQUENCE 595 AA; 63754 MW; B0EE9055097CFBA5 CRC64;
MAATAATTFS LSSSSSTSAA ASKALKQSPK PSALNLGFLG SSSTIKACRS LKAARVLPSG
ANGGGSALSA QMVSAPSINT PSATTFDFDS SVFKKEKVTL SGHDEYIVRG GRNLFPLLPD
AFKGIKQIGV IGWGSQAPAQ AQNLKDSLTE AKSDVVVKIG LRKGSNSFAE ARAAGFSEEN
GTLGDMWETI SGSDLVLLLI SDSAQADNYE KVFSHMKPNS ILGLSHGFLL GHLQSLGQDF
PKNISVIAVC PKGMGPSVRR LYVQGKEVNG AGINSSFAVH QDVDGRATDV ALGWSIALGS
PFTFATTLEQ EYKSDIFGER GILLGAVHGI VECLFRRYTE SGMSEDLAYK NTVECITGVI
SKTISTKGML ALYNSLSEEG KKDFQAAYSA SYYPSMDILY ECYEDVASGS EIRSVVLAGR
RFYEKEGLPA FPMGKIDQTR MWKVGEKVRS VRPAGDLGPL YPFTAGVYVA LMMAQIEILR
KKGHSYSEII NESVIEAVDS LNPFMHARGV SFMVDNCSTT ARLGSRKWAP RFDYILSQQA
LVAVDNGAPI NQDLISNFLS DPVHEAIGVC AQLRPSVDIS VTADADFVRP ELRQA