ILVC_BUCUM
ID ILVC_BUCUM Reviewed; 346 AA.
AC Q9AQA0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000250|UniProtKB:P05793};
DE Short=KARI {ECO:0000250|UniProtKB:P05793};
DE EC=1.1.1.86 {ECO:0000250|UniProtKB:P05793};
DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000250|UniProtKB:P05793};
DE Short=AHIR {ECO:0000250|UniProtKB:P05793};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000250|UniProtKB:P05793};
DE AltName: Full=Ketol-acid reductoisomerase type 2 {ECO:0000250|UniProtKB:P05793};
DE AltName: Full=Ketol-acid reductoisomerase type II {ECO:0000250|UniProtKB:P05793};
DE Flags: Fragment;
GN Name=ilvC;
OS Buchnera aphidicola subsp. Uroleucon ambrosiae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118117;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wernegreen J.J., Moran N.A.;
RT "Accelerated evolutionary rates at biosynthetic loci of Buchnera-
RT Uroleucon.";
RL Submitted (DEC-1999) 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:0000250|UniProtKB:P05793}.
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:0000250|UniProtKB:P05793};
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:0000250|UniProtKB:P05793};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P05793};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:P05793};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC {ECO:0000250|UniProtKB:P05793}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000250|UniProtKB:P05793}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000305}.
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DR EMBL; AF217553; AAK01024.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AQA0; -.
DR SMR; Q9AQA0; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
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:0050661; F:NADP binding; IEA:InterPro.
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; IPR014359; KARI_prok.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21371; PTHR21371; 2.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000116; IlvC_gammaproteo; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00465; ilvC; 1.
DR PROSITE; PS51851; KARI_C; 2.
DR PROSITE; PS51850; KARI_N; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Magnesium;
KW Metal-binding; NADP; Oxidoreductase; Repeat.
FT CHAIN <1..>346
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_0000151295"
FT DOMAIN <1..141
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 142..286
FT /note="KARI C-terminal knotted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT DOMAIN 287..>346
FT /note="KARI C-terminal knotted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 65
FT /evidence="ECO:0000250|UniProtKB:P05793"
FT BINDING 11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P05793"
FT BINDING 41..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P05793"
FT BINDING 91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P05793"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT NON_TER 1
FT NON_TER 346
SQ SEQUENCE 346 AA; 39458 MW; 77BDE5FF866785BA CRC64;
KKNSILKKNQ SWINATENNF KVDDYESLIP NADLVINLTP DKEHHNVVTT LQKLMKKNSY
LGYSHGFNIV EFGEIIRKDI TVIMVAPKCP GTEVREEYKR GFGVPTLIAV HNENDIHQKG
LEIAKAWSFS IGSHRAGVLE SSFIAEVKSD LMGEQTILCG MLQTASILCY EKLITNKHDP
AYAAKLIQNG WETITESLKH GGITLMMDRL SNPSKIRAYK ISEKIKKILT SLFQQHMNNI
ISGEFSSEMM KDWKNNDKKL LDWRKQTKDT SFEKAPIYIK KIPEQEYYDH GILMIAILKA
GIELSFETMI NSGIIAESAY YESLHELPLI ANTIARKKLY EMNKVI
