ID   A1R7L9_PAEAT            Unreviewed;       365 AA.
AC   A1R7L9;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   15-MAR-2017, entry version 86.
DE   RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435};
DE            Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435};
DE            EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435};
DE   AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435};
DE            Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435};
DE   AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435};
GN   Name=ilvC {ECO:0000256|HAMAP-Rule:MF_00435,
GN   ECO:0000313|EMBL:ABM08654.1};
GN   OrderedLocusNames=AAur_2507 {ECO:0000313|EMBL:ABM08654.1};
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08654.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM08654.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM08654.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of
RT   Arthrobacter aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of branched-chain amino
CC       acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-
CC       acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-
CC       dihydroxy-isovalerate. In the isomerase reaction, S2AL is
CC       rearranged via a Mg-dependent methyl migration to produce 3-
CC       hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction,
CC       this 2-ketoacid undergoes a metal-dependent reduction by NADPH to
CC       yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000256|HAMAP-
CC       Rule:MF_00435}.
CC   -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
CC       = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CC       {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00616534}.
CC   -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
CC       NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
CC       {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00616537}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00435};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00435};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00435, ECO:0000256|SAAS:SAAS00677654}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 2/4. {ECO:0000256|HAMAP-Rule:MF_00435,
CC       ECO:0000256|SAAS:SAAS00677656}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00677653}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}.
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DR   EMBL; CP000474; ABM08654.1; -; Genomic_DNA.
DR   ProteinModelPortal; A1R7L9; -.
DR   STRING; 290340.AAur_2507; -.
DR   EnsemblBacteria; ABM08654; ABM08654; AAur_2507.
DR   KEGG; aau:AAur_2507; -.
DR   PATRIC; 20980450; VBIArtAur67810_2540.
DR   eggNOG; ENOG4105C6M; Bacteria.
DR   eggNOG; COG0059; LUCA.
DR   HOGENOM; HOG000016230; -.
DR   KO; K00053; -.
DR   OMA; WEGGIAK; -.
DR   OrthoDB; POG091H063Y; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000000637; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_00435; IlvC; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR013116; IlvN.
DR   InterPro; IPR013023; Ketol-acid_reductoisomrdctse.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR21371; PTHR21371; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00435,
KW   ECO:0000256|SAAS:SAAS00677647};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_00435, ECO:0000256|SAAS:SAAS00677648};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000637};
KW   Isomerase {ECO:0000313|EMBL:ABM08654.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00435,
KW   ECO:0000256|SAAS:SAAS00677517};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435,
KW   ECO:0000256|SAAS:SAAS00677535};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00642978};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00435,
KW   ECO:0000256|SAAS:SAAS00622208};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435,
KW   ECO:0000256|SAAS:SAAS00677651, ECO:0000313|EMBL:ABM08654.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000637}.
FT   DOMAIN       39    202       IlvN. {ECO:0000259|Pfam:PF07991}.
FT   DOMAIN      208    351       IlvC. {ECO:0000259|Pfam:PF01450}.
FT   ACT_SITE    132    132       {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   METAL       215    215       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435}.
FT   METAL       215    215       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435}.
FT   METAL       219    219       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435}.
FT   METAL       251    251       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435}.
FT   METAL       255    255       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435}.
FT   BINDING      72     72       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING      75     75       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING      77     77       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING     158    158       NADP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING     276    276       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435}.
SQ   SEQUENCE   365 AA;  39660 MW;  B9650A5A2BCE9527 CRC64;
     MSLAPSTAAP LSISTKNHSR GVTQVTEMFY DDDADLSIIQ GRKVAIVGYG SQGHAHALNL
     RDSGVEVVIA LKDGSKSTSK AEDAGFTVKN VADAAEWADV IMILAPDQHQ RSIYNDSIKD
     KLTEGKALAF AHGFNIRFGY IEAPAGVDVI LIAPKAPGHT VRREFEAGRG IPDIIAVEQD
     ASGSAWDLAK SYAKAIGGTR AGVIKTTFTE ETETDLFGEQ AVLCGGVSQL VQYGFETLTE
     AGYQPQIAYF EVLHELKLIV DLMWEGGIAK QRWSVSDTAE YGDYVSGPRV ITPEVKENMK
     AVLADIQNGA FAKRFIDDQD NGGTEFKELR AKAEQHPIEE VGRELRSLFS WQQQDADYVE
     GSAAR
//