ILVC_STAA8
ID ILVC_STAA8 Reviewed; 334 AA.
AC Q2FWK4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00435};
DE Short=KARI {ECO:0000255|HAMAP-Rule:MF_00435};
DE EC=1.1.1.86 {ECO:0000255|HAMAP-Rule:MF_00435};
DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000255|HAMAP-Rule:MF_00435};
DE Short=AHIR {ECO:0000255|HAMAP-Rule:MF_00435};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435};
DE AltName: Full=Ketol-acid reductoisomerase type 1 {ECO:0000255|HAMAP-Rule:MF_00435};
DE AltName: Full=Ketol-acid reductoisomerase type I {ECO:0000255|HAMAP-Rule:MF_00435};
GN Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435};
GN OrderedLocusNames=SAOUHSC_02284;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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:0000255|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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00435};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00435};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_00435}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00435}.
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DR EMBL; CP000253; ABD31322.1; -; Genomic_DNA.
DR RefSeq; WP_000214557.1; NZ_LS483365.1.
DR RefSeq; YP_500766.1; NC_007795.1.
DR PDB; 5W3K; X-ray; 1.59 A; A/B=1-334.
DR PDB; 6AQJ; X-ray; 1.37 A; A/B=2-334.
DR PDB; 6BUL; X-ray; 1.88 A; A/B=1-334.
DR PDB; 6C55; X-ray; 2.09 A; A/B=1-334.
DR PDB; 6C5N; X-ray; 1.67 A; A/B=2-334.
DR PDB; 6VO2; X-ray; 1.59 A; A/B=1-334.
DR PDB; 7KE2; X-ray; 2.59 A; A/B=1-334.
DR PDB; 7KH7; X-ray; 2.63 A; A/B=1-334.
DR PDBsum; 5W3K; -.
DR PDBsum; 6AQJ; -.
DR PDBsum; 6BUL; -.
DR PDBsum; 6C55; -.
DR PDBsum; 6C5N; -.
DR PDBsum; 6VO2; -.
DR PDBsum; 7KE2; -.
DR PDBsum; 7KH7; -.
DR AlphaFoldDB; Q2FWK4; -.
DR SMR; Q2FWK4; -.
DR STRING; 1280.SAXN108_2299; -.
DR EnsemblBacteria; ABD31322; ABD31322; SAOUHSC_02284.
DR GeneID; 3919159; -.
DR KEGG; sao:SAOUHSC_02284; -.
DR PATRIC; fig|93061.5.peg.2074; -.
DR eggNOG; COG0059; Bacteria.
DR HOGENOM; CLU_033821_0_1_9; -.
DR OMA; RAMFSWL; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR PRO; PR:Q2FWK4; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_00435; IlvC; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
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; 1.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000116; IlvC_gammaproteo; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00465; ilvC; 1.
DR PROSITE; PS51851; KARI_C; 1.
DR PROSITE; PS51850; KARI_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Magnesium; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_0000252791"
FT DOMAIN 1..181
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 182..327
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 25..28
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 82..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5W3K"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5W3K"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:5W3K"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 200..215
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:5W3K"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:5W3K"
SQ SEQUENCE 334 AA; 36956 MW; 33E0B8FC772DE52E CRC64;
MTTVYYDQDV KTDALQGKKI AVVGYGSQGH AHAQNLKDNG YDVVIGIRPG RSFDKAKEDG
FDVFPVAEAV KQADVIMVLL PDEIQGDVYK NEIEPNLEKH NALAFAHGFN IHFGVIQPPA
DVDVFLVAPK GPGHLVRRTF VEGSAVPSLF GIQQGASGQA RNIALSYAKG IGATRAGVIE
TTFKEETETD LFGEQAVLCG GVSKLIQSGF ETLVEAGYQP ELAYFEVLHE MKLIVDLMYE
GGMENVRYSI SNTAEFGDYV SGPRVITPDV KENMKAVLTD IQNGNFSNRF IEDNKNGFKE
FYKLREEQHG HQIEKVGREL REMMPFIKSK SIEK
