GENTAUR Molecular Products.

 A0A126QXH1_9EURY        Unreviewed;       327 AA.
 A0A126QXH1;
 11-MAY-2016, integrated into UniProtKB/TrEMBL.
 11-MAY-2016, sequence version 1.
 28-MAR-2018, entry version 16.
 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=AUP07_1312 {ECO:0000313|EMBL:AMK14349.1};
 methanogenic archaeon mixed culture ISO4-G1.
 Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
 environmental samples.
 NCBI_TaxID=1452364 {ECO:0000313|EMBL:AMK14349.1};
 [1] {ECO:0000313|EMBL:AMK14349.1}
 NUCLEOTIDE SEQUENCE.
 STRAIN=ISO4-G1 {ECO:0000313|EMBL:AMK14349.1};
 PubMed=27056226;
 Kelly W.J., Li D., Lambie S.C., Jeyanathan J., Cox F., Li Y.,
 Attwood G.T., Altermann E., Leahy S.C.;
 "Complete Genome Sequence of Methanogenic Archaeon ISO4-G1, a Member
 of the Methanomassiliicoccales, Isolated from a Sheep Rumen.";
 Genome Announc. 4:0-0(2016).
 -!- 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}.
 -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
     = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
     {ECO:0000256|HAMAP-Rule:MF_00435}.
 -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
     NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
     {ECO:0000256|HAMAP-Rule:MF_00435}.
 -!- 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}.
 -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
     from pyruvate: step 2/4. {ECO:0000256|HAMAP-Rule:MF_00435}.
 -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
     {ECO:0000256|HAMAP-Rule:MF_00435}.
 -!- CAUTION: Lacks conserved residue(s) required for the propagation
     of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}.
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 EMBL; CP013703; AMK14349.1; -; Genomic_DNA.
 PATRIC; fig|1452364.3.peg.1344; -.
 UniPathway; UPA00047; UER00056.
 UniPathway; UPA00049; UER00060.
 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; IPR000506; AcH_isomrdctse_C.
 InterPro; IPR013116; IlvN.
 InterPro; IPR013023; KARI.
 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; 1.
 SUPFAM; SSF48179; SSF48179; 1.
 SUPFAM; SSF51735; SSF51735; 1.
 TIGRFAMs; TIGR00465; ilvC; 1.
 3: Inferred from homology;
 Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00435};
 Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
 Rule:MF_00435}; Coiled coil {ECO:0000256|SAM:Coils};
 Isomerase {ECO:0000313|EMBL:AMK14349.1};
 Magnesium {ECO:0000256|HAMAP-Rule:MF_00435};
 Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435};
 NADP {ECO:0000256|HAMAP-Rule:MF_00435};
 Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435}.
 DOMAIN       14    177       IlvN. {ECO:0000259|Pfam:PF07991}.
 DOMAIN      183    324       IlvC. {ECO:0000259|Pfam:PF01450}.
 NP_BIND      24     27       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
 COILED      301    321       {ECO:0000256|SAM:Coils}.
 ACT_SITE    107    107       {ECO:0000256|HAMAP-Rule:MF_00435}.
 METAL       190    190       Magnesium 1. {ECO:0000256|HAMAP-
                              Rule:MF_00435}.
 METAL       190    190       Magnesium 2. {ECO:0000256|HAMAP-
                              Rule:MF_00435}.
 METAL       194    194       Magnesium 1. {ECO:0000256|HAMAP-
                              Rule:MF_00435}.
 METAL       226    226       Magnesium 2. {ECO:0000256|HAMAP-
                              Rule:MF_00435}.
 METAL       230    230       Magnesium 2. {ECO:0000256|HAMAP-
                              Rule:MF_00435}.
 BINDING      47     47       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}.
 SEQUENCE   327 AA;  35940 MW;  D1AE6C108139ABF3 CRC64;
 MQLYHDGDVD LSIFEGKKVA VLGYGSQGRA QALCFHDSGM DVTVGVRRNG PSWNQAKEDG
 LKVAELADAV KGADVVVVLL PDEVQASVYK ESVGPNLKSG AALAFAHGFA ITFKTIVPPK
 DVDVIMMAPK GPGNMVRQIF LEGFGVPAMV CINQDHTGNA MKIALGLAKG IGATRSGVFE
 STFERETHTD LFGEQAVLCG GQTGLIKNGF ETLVEAGYPP EMAYFEVLHE MKQVTELINR
 GGLDLMWHEV SNTAEFGGLT RRDRVVNESS KEEMRKILKE IQDGTFKNEW VSEFDNGLVN
 LKRMEDEEAK LQMEVVGKEI RRLFQRK

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