ID   A1ST80_PSYIN            Unreviewed;       493 AA.
AC   A1ST80;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 128.
DE   RecName: Full=Ketol-acid reductoisomerase {ECO:0000256|NCBIfam:TIGR00465};
DE            EC=1.1.1.86 {ECO:0000256|NCBIfam:TIGR00465};
GN   OrderedLocusNames=Ping_0853 {ECO:0000313|EMBL:ABM02695.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02695.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM02695.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM02695.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC         acetolactate + NADPH + H(+); 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|ARBA:ARBA00049021};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004885}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00010318, 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; CP000510; ABM02695.1; -; Genomic_DNA.
DR   RefSeq; WP_011769258.1; NC_008709.1.
DR   AlphaFoldDB; A1ST80; -.
DR   STRING; 357804.Ping_0853; -.
DR   KEGG; pin:Ping_0853; -.
DR   eggNOG; COG0059; Bacteria.
DR   HOGENOM; CLU_551905_0_0_6; -.
DR   OrthoDB; 9804088at2; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000000639; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00465; ilvC; 1.
DR   NCBIfam; NF003557; PRK05225.1; 1.
DR   PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01450; KARI_C; 2.
DR   Pfam; PF07991; KARI_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
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|PROSITE-ProRule:PRU01198};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|PROSITE-ProRule:PRU01198};
KW   Isomerase {ECO:0000313|EMBL:ABM02695.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PROSITE-
KW   ProRule:PRU01198};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01198}; NADP {ECO:0000256|PROSITE-ProRule:PRU01197};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|PROSITE-
KW   ProRule:PRU01198}; Reference proteome {ECO:0000313|Proteomes:UP000000639}.
FT   DOMAIN          14..208
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          209..353
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   DOMAIN          355..486
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01197"
FT   BINDING         45..48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01197"
FT   BINDING         68
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01197"
FT   BINDING         78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01197"
FT   BINDING         158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01197"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         389
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         393
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ   SEQUENCE   493 AA;  54400 MW;  2B3B43B3FC22C9CE CRC64;
     MANYFNTLSL REKLNQLGQC RFMDRSEFTD GCDALKGKKV VIIGCGAQGL NQGLNMRDSG
     LDVSYTLRAQ AIAEKRQSWK NATENGFVVG TYEELIPEAD LLCNLTPDKQ HTAVVGAVMP
     LMKEGATLSY SHGFNIVEEG MQVREDLTVI MCAPKCPGSE VREEYKRGFG VPTLIAVHPA
     NDPQGQGLVW AKAYASATGG DRAGVLMSSF VAEVKSDLMG EQTILCGMLQ TGAIIGYEKM
     VADGIEPGYA SKLIQYGWET VTEGMKYGGI TNMMDRLSNP AKIKAFDMSL ELKEILRPLF
     NKHMDDIIEG EFSRTMMEDW ANDDKNLLQW RAETAETGFE KQPAGDMKID EQEFYDNGIF
     LIAMIKAGVE LAFDAMTASG IIADSAYYES LHETPLIANT IARKKLYEMN VVISDTAEYG
     CYLFDHAAKP LLADFVKALD PEMLGKPLTV KNNAVDNARL IEVNEAIRSH PVEIVGKKLR
     GYMTEMKTII TAS
//