ILVC_SULAC
ID ILVC_SULAC Reviewed; 332 AA.
AC Q4J8K9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=Saci_1559;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80872.1; -; Genomic_DNA.
DR RefSeq; WP_011278374.1; NC_007181.1.
DR PDB; 5YEQ; X-ray; 1.75 A; A/B=1-332.
DR PDBsum; 5YEQ; -.
DR AlphaFoldDB; Q4J8K9; -.
DR SMR; Q4J8K9; -.
DR STRING; 330779.Saci_1559; -.
DR EnsemblBacteria; AAY80872; AAY80872; Saci_1559.
DR GeneID; 3474594; -.
DR KEGG; sai:Saci_1559; -.
DR PATRIC; fig|330779.12.peg.1499; -.
DR eggNOG; arCOG04465; Archaea.
DR HOGENOM; CLU_033821_0_1_2; -.
DR OMA; RAMFSWL; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000001018; Chromosome.
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:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
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..332
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_0000151399"
FT DOMAIN 2..182
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 183..328
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 108
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 53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 83..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5YEQ"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5YEQ"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:5YEQ"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:5YEQ"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 232..250
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:5YEQ"
FT HELIX 313..328
FT /evidence="ECO:0007829|PDB:5YEQ"
SQ SEQUENCE 332 AA; 36922 MW; 69C000D490FE1F0C CRC64;
MAKIYTDKDV SLDVIKEKRV AVLGYGSQGR AWALNLRDSG IKVSVGLERE GNSWKQAEND
GFKPLRTEEA VRNSDIIIFL LPDMIQRTVY LERVKPYLKE GMDLVFAHGF NIHYRLIEPP
SNVDVYMIAP KAPGPIVREY FAKGGGVPAL VATYQDHSGK ALQKALAVAK AIGATRAGVI
ETTFKEETET DLFGEQVDLV GGVMQLMRYA FQTLVEAGYQ PEVAYFETIN EMKLIVDLVY
EKGFSGMLTA VSDTAKYGGM TVGKMVIDES VKERMKKALD NIRSGKFAEK WVEEYGKGAN
TIKEGMKEVD NSTEEKVGRS LRDIILRGKP KS
