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Ketol-acid reductoisomerase (NADP( )) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase)

 A0A0A3IZZ7_9BACI        Unreviewed;       337 AA.
A0A0A3IZZ7;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
08-MAY-2019, entry version 37.
RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435};
Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435};
EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435};
AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435};
Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435};
AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435};
Name=ilvC {ECO:0000256|HAMAP-Rule:MF_00435};
ORFNames=CD30_12165 {ECO:0000313|EMBL:KGR90319.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR90319.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR90319.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR90319.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the biosynthesis of branched-chain amino
acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-
acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-
dihydroxy-isovalerate. In the isomerase reaction, S2AL is
rearranged via a Mg-dependent methyl migration to produce 3-
hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction,
this 2-ketoacid undergoes a metal-dependent reduction by NADPH to
yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|SAAS:SAAS00992119}.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068,
ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783,
ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86;
Evidence={ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS01120909};
-!- CATALYTIC ACTIVITY:
Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-
2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH;
Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256,
ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
EC=1.1.1.86; Evidence={ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS01120914};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00435};
Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_00435};
-!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|SAAS:SAAS00320659}.
-!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
from pyruvate: step 2/4. {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|SAAS:SAAS00320673}.
-!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
{ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198, ECO:0000256|SAAS:SAAS00556475}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR90319.1}.
-----------------------------------------------------------------------
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EMBL; JPVQ01000021; KGR90319.1; -; Genomic_DNA.
RefSeq; WP_036177137.1; NZ_JPVQ01000021.1.
STRING; 1211035.CD30_12165; -.
EnsemblBacteria; KGR90319; KGR90319; CD30_12165.
OrthoDB; 188901at2; -.
UniPathway; UPA00047; UER00056.
UniPathway; UPA00049; UER00060.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_00435; IlvC; 1.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR013023; KARI.
InterPro; IPR000506; KARI_C.
InterPro; IPR013116; KARI_N.
InterPro; IPR014359; KARI_prok.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR21371; PTHR21371; 1.
Pfam; PF01450; IlvC; 1.
Pfam; PF07991; IlvN; 1.
PIRSF; PIRSF000116; IlvC_gammaproteo; 2.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00465; ilvC; 1.
PROSITE; PS51851; KARI_C; 1.
PROSITE; PS51850; KARI_N; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00435,
ECO:0000256|PROSITE-ProRule:PRU01198, ECO:0000256|SAAS:SAAS00320675};
Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|PROSITE-ProRule:PRU01198,
ECO:0000256|SAAS:SAAS00320675};
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Isomerase {ECO:0000313|EMBL:KGR90319.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198, ECO:0000256|SAAS:SAAS00825999};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198, ECO:0000256|SAAS:SAAS00825953};
NADP {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00993879};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198, ECO:0000256|SAAS:SAAS00320678,
ECO:0000313|EMBL:KGR90319.1};
Reference proteome {ECO:0000313|Proteomes:UP000030595}.
DOMAIN 2 181 KARI N-terminal Rossmann.
{ECO:0000259|PROSITE:PS51850}.
DOMAIN 182 327 KARI C-terminal knotted.
{ECO:0000259|PROSITE:PS51851}.
NP_BIND 25 28 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
ACT_SITE 107 107 {ECO:0000256|HAMAP-Rule:MF_00435}.
METAL 190 190 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198}.
METAL 190 190 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198}.
METAL 194 194 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198}.
METAL 226 226 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198}.
METAL 230 230 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198}.
BINDING 48 48 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
BINDING 52 52 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
BINDING 133 133 NADP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00435}.
BINDING 251 251 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00435, ECO:0000256|PROSITE-
ProRule:PRU01198}.
SEQUENCE 337 AA; 37111 MW; 484EDF0CB964EC1E CRC64;
MAKMYYQNEI NDSVLRGKKI AIIGYGSQGH AHAQNLKESG FDVVVGVRPG KSFDQAKEDG
LDVRTVAEAA EVADIIQILL PDERQKAVYE EEIAPNLKSG NALMFAHGFN INFGQIVPPA
DVDVFLVAPK GPGHLVRRTY AQGAGVPALF AIFQDATGEA RDLALAYGKG IGAARAGMLE
TTFKEETETD LFGEQAVLCG GTTQLVKYGF ETLVEAGYQP ELAYFETLHE LKLIVDLMYE
GGMATMRYSI SDTAEWGDYV SGPRIIDPSV KERMKDVLTD IQNGTFAKDW INENETGRPR
YTEYKKAGAE HQIEEVGSKL REMMPFINEG KKKVVVK


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Bibliography :