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Ketol-acid reductoisomerase (NAD( )) (KARI) (EC 1.1.1.382) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 1) (Ketol-acid reductoisomerase type I)

 ILVC_UNCAG              Reviewed;         332 AA.
Q64BR7;
06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 1.
23-MAY-2018, entry version 70.
RecName: Full=Ketol-acid reductoisomerase (NAD(+)) {ECO:0000303|PubMed:25849365};
Short=KARI {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:25849365};
EC=1.1.1.382 {ECO:0000250|UniProtKB:K4LVZ1};
AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000255|HAMAP-Rule:MF_00435};
Short=AHIR {ECO:0000255|HAMAP-Rule:MF_00435};
AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435};
AltName: Full=Ketol-acid reductoisomerase type 1 {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:25849365};
AltName: Full=Ketol-acid reductoisomerase type I {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:25849365};
Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435};
ORFNames=GZ26G2_30 {ECO:0000312|EMBL:AAU83160.1};
Uncultured archaeon GZfos26G2.
Archaea; environmental samples.
NCBI_TaxID=285389;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15353801; DOI=10.1126/science.1100025;
Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
Richardson P.M., DeLong E.F.;
"Reverse methanogenesis: testing the hypothesis with environmental
genomics.";
Science 305:1457-1462(2004).
[2]
X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) IN COMPLEX WITH NAD AND
MAGNESIUM IONS, FUNCTION, COFACTOR, AND SUBUNIT.
PubMed=25849365; DOI=10.1042/BJ20150183;
Cahn J.K., Brinkmann-Chen S., Spatzal T., Wiig J.A., Buller A.R.,
Einsle O., Hu Y., Ribbe M.W., Arnold F.H.;
"Cofactor specificity motifs and the induced fit mechanism in class I
ketol-acid reductoisomerases.";
Biochem. J. 468:475-484(2015).
-!- 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 NADH to
yield (R)-2,3-dihydroxy-isovalerate.
{ECO:0000269|PubMed:25849365}.
-!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+)
= (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADH.
{ECO:0000250|UniProtKB:K4LVZ1}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:25849365};
Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
Rule:MF_00435};
-!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
Rule:MF_00435}.
-!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25849365}.
-!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
{ECO:0000255|HAMAP-Rule:MF_00435}.
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EMBL; AY714843; AAU83160.1; -; Genomic_DNA.
PDB; 4XDY; X-ray; 1.53 A; A/B=1-332.
PDBsum; 4XDY; -.
ProteinModelPortal; Q64BR7; -.
SMR; Q64BR7; -.
UniPathway; UPA00047; UER00056.
UniPathway; UPA00049; UER00060.
GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00465; ilvC; 1.
PROSITE; PS51851; KARI_C; 1.
PROSITE; PS51850; KARI_N; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis;
Branched-chain amino acid biosynthesis; Magnesium; Metal-binding; NAD;
Oxidoreductase.
CHAIN 1 332 Ketol-acid reductoisomerase (NAD(+)).
/FTId=PRO_0000436836.
DOMAIN 1 186 KARI N-terminal Rossmann.
{ECO:0000255|PROSITE-ProRule:PRU01197}.
DOMAIN 187 332 KARI C-terminal knotted.
{ECO:0000255|PROSITE-ProRule:PRU01198}.
NP_BIND 24 27 NAD. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
NP_BIND 87 90 NAD. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
ACT_SITE 112 112 {ECO:0000255|HAMAP-Rule:MF_00435}.
METAL 195 195 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
METAL 195 195 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00435}.
METAL 199 199 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
METAL 231 231 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00435}.
METAL 235 235 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00435}.
BINDING 46 46 NAD. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
BINDING 55 55 NAD. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
BINDING 57 57 NAD. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
BINDING 138 138 NAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:25849365}.
BINDING 256 256 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00435}.
HELIX 6 8 {ECO:0000244|PDB:4XDY}.
HELIX 12 16 {ECO:0000244|PDB:4XDY}.
STRAND 18 22 {ECO:0000244|PDB:4XDY}.
HELIX 26 37 {ECO:0000244|PDB:4XDY}.
STRAND 41 46 {ECO:0000244|PDB:4XDY}.
STRAND 48 50 {ECO:0000244|PDB:4XDY}.
HELIX 56 63 {ECO:0000244|PDB:4XDY}.
STRAND 67 70 {ECO:0000244|PDB:4XDY}.
HELIX 71 77 {ECO:0000244|PDB:4XDY}.
STRAND 79 83 {ECO:0000244|PDB:4XDY}.
TURN 87 89 {ECO:0000244|PDB:4XDY}.
HELIX 90 97 {ECO:0000244|PDB:4XDY}.
HELIX 99 101 {ECO:0000244|PDB:4XDY}.
STRAND 107 113 {ECO:0000244|PDB:4XDY}.
HELIX 114 117 {ECO:0000244|PDB:4XDY}.
STRAND 127 136 {ECO:0000244|PDB:4XDY}.
HELIX 138 146 {ECO:0000244|PDB:4XDY}.
STRAND 153 159 {ECO:0000244|PDB:4XDY}.
HELIX 165 175 {ECO:0000244|PDB:4XDY}.
HELIX 178 180 {ECO:0000244|PDB:4XDY}.
STRAND 183 185 {ECO:0000244|PDB:4XDY}.
HELIX 188 201 {ECO:0000244|PDB:4XDY}.
TURN 202 204 {ECO:0000244|PDB:4XDY}.
HELIX 205 220 {ECO:0000244|PDB:4XDY}.
HELIX 225 232 {ECO:0000244|PDB:4XDY}.
HELIX 234 254 {ECO:0000244|PDB:4XDY}.
HELIX 257 270 {ECO:0000244|PDB:4XDY}.
HELIX 273 287 {ECO:0000244|PDB:4XDY}.
HELIX 290 300 {ECO:0000244|PDB:4XDY}.
HELIX 304 315 {ECO:0000244|PDB:4XDY}.
HELIX 317 327 {ECO:0000244|PDB:4XDY}.
SEQUENCE 332 AA; 36857 MW; D5904ACF0CB78E4D CRC64;
MEILHDEDVD DSILRDKTIA VMGYGAQGDA QANCLKDSGI NVVIGETEIL GGNKNPSWEK
AKEDGFEVLP IDKAAEKGDV VHILLPDEVQ PAIYENQIKP QLKAGKALCF SHGFNICFKR
IVPPEDVDVI MVAPKAPGTE ERKAYLEGFG VPGLVAVKQN PSGEAREVAL AMTKAMHWTK
AGILECTFEQ ETYEDLFGEQ CVLCGGLVEL MRNGFEVLVE AGYPPEMAYF ECVHEMKLIV
DLVWQGGIKR MAEVISNTAE YGMWAVGHQI IGPEVKEKMK EALKRVENGE FANEWVDEYK
RGIPFLKASR EKMGEHQVET VGAEIRKLFA QK


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