ILV5_PEA
ID ILV5_PEA Reviewed; 581 AA.
AC O82043;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=PGAAIR;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. G2;
RA Gu X., Xu Y., Wu J., Hou X., Chen Z., Zhu Y.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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; 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.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; Y17796; CAA76854.1; -; mRNA.
DR PIR; T06825; T06825.
DR AlphaFoldDB; O82043; -.
DR SMR; O82043; -.
DR PRIDE; O82043; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Magnesium; Metal-binding; NADP; Oxidoreductase; Plastid;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..581
FT /note="Ketol-acid reductoisomerase, chloroplastic"
FT /id="PRO_0000015630"
FT DOMAIN 92..290
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 291..439
FT /note="KARI C-terminal knotted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT DOMAIN 440..576
FT /note="KARI C-terminal knotted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 210
FT /evidence="ECO:0000255"
FT BINDING 113..120
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 146..151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 185..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 502
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 581 AA; 62852 MW; D6F2B8DF4B2AC697 CRC64;
MAAVTSSCST AISASSKTLA KPVAASFAPT NLSFSKLSPQ SIRARRSITV GSALGATKVS
APPATHPVSL DFETSVFKKE RVNLAGHEEY IVRGGRDLFH LLPDAFKGIK QIGVIGWGSQ
GPAQAQNLRD SLVEAKSDIV VKVGLRKGSS SFNEAREAGF SEEKGTLGDI WETISGSDLV
LLLISDSAQA DNYEKIFSHL KPNSILGLSH GFLLGHLQSI GLDFPKNFSV IAVCPKGMGP
SVRRLYVQGK EINGAGINSS FGVHQDVDGR ATNVALGWSV ALGSPFTFAT TLEQEYKSDI
FGERGILLGA VHGIVESLFR RYTENGMSED LAYKNTVESI TGVISKTIST QGMLAVYNAL
SEDGKKEFEK AYSASFYPCM EILYECYEDV ASGSEIRSVV LAGRRFYEKE GLPAFPMGKI
DQTRMWKVGE RVRSTRPAGD LGPLYPFTAG VFVAMMMAQI EVLRKKGHSY SEIINESVIE
SVDSLNPFMH ARGVSFMVDN CSTTARLGSR KWAPRFDYIL TQQALVAVDS GAPINQDLIS
NFVSDPVHGA IQVCAELRPT LDISVPAAAD FVRPELRQCS N
