ID A1R7L9_PAEAT Unreviewed; 365 AA. AC A1R7L9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 18-SEP-2019, entry version 109. 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, ECO:0000256|SAAS:SAAS00992119}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2- CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00435, CC ECO:0000256|SAAS:SAAS01120909}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)- CC 2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; CC Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, CC ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.86; Evidence={ECO:0000256|HAMAP-Rule:MF_00435, CC ECO:0000256|SAAS:SAAS01120914}; 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:SAAS00320659}. 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:SAAS00320673}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- CC ProRule:PRU01198, ECO:0000256|SAAS:SAAS00556475}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000474; ABM08654.1; -; Genomic_DNA. DR STRING; 290340.AAur_2507; -. DR EnsemblBacteria; ABM08654; ABM08654; AAur_2507. DR KEGG; aau:AAur_2507; -. DR eggNOG; ENOG4105C6M; Bacteria. DR eggNOG; COG0059; LUCA. DR HOGENOM; HOG000016230; -. DR KO; K00053; -. DR OMA; RAMFSWL; -. 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-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; 2. 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00435, KW ECO:0000256|PROSITE-ProRule:PRU01198, ECO:0000256|SAAS:SAAS00320664}; KW Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP- KW Rule:MF_00435, ECO:0000256|PROSITE-ProRule:PRU01198, KW ECO:0000256|SAAS:SAAS00320675}; KW Complete proteome {ECO:0000313|Proteomes:UP000000637}; KW Isomerase {ECO:0000313|EMBL:ABM08654.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198, ECO:0000256|SAAS:SAAS00825999}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198, ECO:0000256|SAAS:SAAS00825953}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00993879}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198, ECO:0000256|SAAS:SAAS00320678, KW ECO:0000313|EMBL:ABM08654.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000637}. FT DOMAIN 26 206 KARI N-terminal Rossmann. FT {ECO:0000259|PROSITE:PS51850}. FT DOMAIN 207 352 KARI C-terminal knotted. FT {ECO:0000259|PROSITE:PS51851}. FT NP_BIND 49 52 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}. FT ACT_SITE 132 132 {ECO:0000256|HAMAP-Rule:MF_00435}. FT METAL 215 215 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 215 215 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 219 219 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 251 251 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 255 255 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. 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, ECO:0000256|PROSITE-ProRule: FT PRU01198}. 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 //