ILVC_STRP2
ID ILVC_STRP2 Reviewed; 340 AA.
AC Q04M32;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=SPD_0406;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ55451.1; -; Genomic_DNA.
DR RefSeq; WP_000218054.1; NC_008533.2.
DR PDB; 6L2I; X-ray; 1.69 A; A/B=1-340.
DR PDB; 6L2K; X-ray; 1.95 A; A/B=1-340.
DR PDB; 6L2R; X-ray; 2.02 A; A/B=1-340.
DR PDB; 6L2S; X-ray; 2.29 A; A/B=1-340.
DR PDB; 6L2Z; X-ray; 2.02 A; A/B=1-340.
DR PDBsum; 6L2I; -.
DR PDBsum; 6L2K; -.
DR PDBsum; 6L2R; -.
DR PDBsum; 6L2S; -.
DR PDBsum; 6L2Z; -.
DR AlphaFoldDB; Q04M32; -.
DR SMR; Q04M32; -.
DR STRING; 373153.SPD_0406; -.
DR EnsemblBacteria; ABJ55451; ABJ55451; SPD_0406.
DR GeneID; 60232911; -.
DR KEGG; spd:SPD_0406; -.
DR eggNOG; COG0059; Bacteria.
DR HOGENOM; CLU_033821_0_1_9; -.
DR OMA; RAMFSWL; -.
DR OrthoDB; 188901at2; -.
DR BioCyc; SPNE373153:G1G6V-445-MON; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000001452; 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.
FT CHAIN 1..340
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_1000050578"
FT DOMAIN 3..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 26..29
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 49
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 8..10
FT /evidence="ECO:0007829|PDB:6L2I"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6L2I"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:6L2I"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:6L2I"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 232..250
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:6L2I"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:6L2I"
SQ SEQUENCE 340 AA; 37350 MW; 1637CC97822470AC CRC64;
MTVQMEYEKD VKVAALDGKK IAVIGYGSQG HAHAQNLRDS GRDVIIGVRP GKSFDKAKED
GFDTYTVAEA TKLADVIMIL APDEIQQELY EAEIAPNLEA GNAVGFAHGF NIHFEFIKVP
ADVDVFMCAP KGPGHLVRRT YEEGFGVPAL YAVYQDATGN AKNIAMDWCK GVGAARVGLL
ETTYKEETEE DLFGEQAVLC GGLTALIEAG FEVLTEAGYA PELAYFEVLH EMKLIVDLIY
EGGFKKMRQS ISNTAEYGDY VSGPRVITEQ VKENMKAVLA DIQNGKFAND FVNDYKAGRP
KLTAYREQAA NLEIEKVGAE LRKAMPFVGK NDDDAFKIYN
