ILVC_PSEAE
ID ILVC_PSEAE Reviewed; 338 AA.
AC Q9HVA2;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
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:0000303|PubMed:12691757};
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:0000303|PubMed:12691757};
DE AltName: Full=Ketol-acid reductoisomerase type I {ECO:0000303|PubMed:12691757};
GN Name=ilvC; OrderedLocusNames=PA4694;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND SUBUNIT.
RX PubMed=12691757; DOI=10.1016/s0022-2836(03)00264-x;
RA Ahn H.J., Eom S.J., Yoon H.J., Lee B.I., Cho H., Suh S.W.;
RT "Crystal structure of class I acetohydroxy acid isomeroreductase from
RT Pseudomonas aeruginosa.";
RL J. Mol. Biol. 328:505-515(2003).
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 -!- SUBUNIT: Dodecamer. {ECO:0000269|PubMed:12691757}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00435}.
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DR EMBL; AE004091; AAG08080.1; -; Genomic_DNA.
DR PIR; E83059; E83059.
DR RefSeq; NP_253382.1; NC_002516.2.
DR RefSeq; WP_003095066.1; NZ_QZGE01000018.1.
DR PDB; 1NP3; X-ray; 2.00 A; A/B/C/D=1-338.
DR PDBsum; 1NP3; -.
DR AlphaFoldDB; Q9HVA2; -.
DR SMR; Q9HVA2; -.
DR STRING; 287.DR97_2036; -.
DR PaxDb; Q9HVA2; -.
DR PRIDE; Q9HVA2; -.
DR EnsemblBacteria; AAG08080; AAG08080; PA4694.
DR GeneID; 881483; -.
DR KEGG; pae:PA4694; -.
DR PATRIC; fig|208964.12.peg.4917; -.
DR PseudoCAP; PA4694; -.
DR HOGENOM; CLU_033821_0_1_6; -.
DR InParanoid; Q9HVA2; -.
DR OMA; RAMFSWL; -.
DR PhylomeDB; Q9HVA2; -.
DR BioCyc; PAER208964:G1FZ6-4798-MON; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR EvolutionaryTrace; Q9HVA2; -.
DR Proteomes; UP000002438; 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..338
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_0000151342"
FT DOMAIN 1..181
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197,
FT ECO:0000305|PubMed:12691757"
FT DOMAIN 182..327
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198,
FT ECO:0000305|PubMed:12691757"
FT ACT_SITE 107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 24..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 50
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 6..8
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1NP3"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1NP3"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 200..215
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:1NP3"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 231..249
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:1NP3"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:1NP3"
SQ SEQUENCE 338 AA; 36425 MW; 93CF5F7DA9F61B0A CRC64;
MRVFYDKDCD LSIIQGKKVA IIGYGSQGHA HACNLKDSGV DVTVGLRSGS ATVAKAEAHG
LKVADVKTAV AAADVVMILT PDEFQGRLYK EEIEPNLKKG ATLAFAHGFS IHYNQVVPRA
DLDVIMIAPK APGHTVRSEF VKGGGIPDLI AIYQDASGNA KNVALSYACG VGGGRTGIIE
TTFKDETETD LFGEQAVLCG GCVELVKAGF ETLVEAGYAP EMAYFECLHE LKLIVDLMYE
GGIANMNYSI SNNAEYGEYV TGPEVINAES RAAMRNALKR IQDGEYAKMF ITEGAANYPS
MTAYRRNNAA HPIEQIGEKL RAMMPWIAAN KIVDKSKN
