ID A0A2S9I5E3_9GAMM Unreviewed; 492 AA.
AC A0A2S9I5E3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435};
DE Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435};
DE EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435};
DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435};
DE Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435};
GN Name=ilvC {ECO:0000256|HAMAP-Rule:MF_00435};
GN ORFNames=CQW29_23265 {ECO:0000313|EMBL:PRD13016.1};
OS Pantoea coffeiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1465635 {ECO:0000313|EMBL:PRD13016.1, ECO:0000313|Proteomes:UP000239181};
RN [1] {ECO:0000313|EMBL:PRD13016.1, ECO:0000313|Proteomes:UP000239181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:PRD13016.1,
RC ECO:0000313|Proteomes:UP000239181};
RA Siqueira K.A., Liotti R.G., Mendes T.A., Soares M.A.;
RT "Draft genome of two endophytic bacteria isolated from 'guarana' Paullinia
RT cupana (Mart.) Ducke.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids
CC (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction
CC of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In
CC the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl
CC migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the
CC reductase reaction, this 2-ketoacid undergoes a metal-dependent
CC reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
CC {ECO:0000256|HAMAP-Rule:MF_00435}.
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|ARBA:ARBA00000507, ECO:0000256|HAMAP-
CC Rule:MF_00435};
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|ARBA:ARBA00000850, ECO:0000256|HAMAP-
CC Rule:MF_00435};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00435};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00435};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004885, ECO:0000256|HAMAP-Rule:MF_00435}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864, ECO:0000256|HAMAP-
CC Rule:MF_00435}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|HAMAP-Rule:MF_00435,
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRD13016.1}.
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DR EMBL; PDET01000023; PRD13016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9I5E3; -.
DR OrthoDB; 9804088at2; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000239181; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium 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 HAMAP; MF_00435; IlvC; 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 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 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, ECO:0000256|HAMAP-
KW Rule:MF_00435};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_00435}; Isomerase {ECO:0000313|EMBL:PRD13016.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00435};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00435};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00435}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 15..208
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 209..344
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT DOMAIN 345..485
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT BINDING 45..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT BINDING 68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT BINDING 108..110
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT BINDING 158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT 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|HAMAP-Rule:MF_00435,
FT 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|HAMAP-Rule:MF_00435,
FT 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|HAMAP-Rule:MF_00435,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 492 AA; 53868 MW; FF8481B0D2A461A4 CRC64;
MSNYFNTLNL RNQLAQLGKC RFMAREEFAD EASYLKGKKV VIVGCGAQGL NQGLNMRDSG
LNISYALRAE AIAEKRASWR KATENGFQVG TYEDLIPQAD LVVNLTPDKQ HSSVVQAVQP
LMKDGAALGY SHGFNIVEVG EQIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
NDPKGEGMAI AKAWAAATGG HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL
VAEGTDAAYA EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKTIMAPLF
QKHMDDIISG EFSSGMMADW ANDDKNLLGW REETGKTAFE TAPQFEGKIA EQTYFDEGVV
MVAMVKAGVE LAFETMLDAG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG
NYLFSYAAVP LLKEFMTTLQ AGDLGKAAST STTVDNAQLR DVNEAIRQHP IESVGRTLRG
YMTDMKRIAV AG
//
