ID A0A0S3SHN9_PHAAN Unreviewed; 582 AA.
AC A0A0S3SHN9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Ketol-acid reductoisomerase {ECO:0000256|PIRNR:PIRNR000118};
DE EC=1.1.1.86 {ECO:0000256|PIRNR:PIRNR000118};
DE AltName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000256|PIRNR:PIRNR000118};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|PIRNR:PIRNR000118};
GN Name=Vigan.07G104900 {ECO:0000313|EMBL:BAT92351.1};
GN ORFNames=VIGAN_07104900 {ECO:0000313|EMBL:BAT92351.1};
OS Vigna angularis var. angularis.
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT92351.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT92351.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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:0000256|PIRNR:PIRNR000118};
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 Evidence={ECO:0000256|PIRNR:PIRNR000118};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR000118};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR000118};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004885, ECO:0000256|PIRNR:PIRNR000118}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864,
CC ECO:0000256|PIRNR:PIRNR000118}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000118}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PIRNR:PIRNR000118,
CC ECO:0000256|PROSITE-ProRule:PRU01198}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01198}.
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DR EMBL; AP015040; BAT92351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SHN9; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000291084; Chromosome 7.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01450; IlvC; 2.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000118; Ilv5_plant; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51851; KARI_C; 2.
DR PROSITE; PS51850; KARI_N; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR000118};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|PIRNR:PIRNR000118};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000118};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000118}; NADP {ECO:0000256|PIRNR:PIRNR000118};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000118};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 93..291
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 292..440
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT DOMAIN 451..577
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT ACT_SITE 211
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-1"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-2,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-2,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-2,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 503
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 582 AA; 63081 MW; 6EA782BA654221C2 CRC64;
MAAATTSCSS AISAASETLA KPSSRSFSAT SLALQSSSSK LTFKSLKLSR CGAALGARMV
AAPAVKAPTQ LDFDTKVFKK EKVNLAGHDE YIVRGGRDLF HFLPDAFKGI KQIGVIGWGS
QGPAQAQNLR DSLAEAKSDI VVKIGLRKGS RSFAEARAAG FTEENGTLGD IWETVSGSDL
VMLLISDSAQ ADNYEKIFSH MKPNSILGLS HGFLLGHLQS IGLDFPQNIS VIAVCPKGMG
PSVRRLYVQG KEINGAGINA SFAVHQDVDG RATDVALGWS VALGSPFTFA TTLEQEYKSD
IFGERGILLG AVHGVVESLF RRYTDNGMDE DLAYKNTVES ITGIISKTIS TKGMLAVYNA
LSEDEKREFE KAYSASYYPC MDILYECYED VASGSEIRSV VLAGRRFYEK EGLPAFPMGN
IDQTRMWKVG ERVRSTRPAG DQGPLYPFTA GVFVALMMAQ IEILRKKGHS YSEIINESVI
EAVDSLNPFM HARGVSFMVD NCSTTARLGS RKWAPRFDYI LTQQALVAVD NGTPVNQDLL
SNFLSDPVHG AIEVCAKLRP TVDISVPADA DFVRPELRHS SN
//
