ID A0A417GL56_9CLOT Unreviewed; 331 AA. AC A0A417GL56; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 29-SEP-2021, entry version 9. 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 ORFNames=DW766_06150 {ECO:0000313|EMBL:RHT56989.1}; OS Butyricicoccus sp. AM29-23AC. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; OC Butyricicoccus; unclassified Butyricicoccus. OX NCBI_TaxID=2292295 {ECO:0000313|EMBL:RHT56989.1, ECO:0000313|Proteomes:UP000286445}; RN [1] {ECO:0000313|EMBL:RHT56989.1, ECO:0000313|Proteomes:UP000286445} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM29-23AC {ECO:0000313|EMBL:RHT56989.1, RC ECO:0000313|Proteomes:UP000286445}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids CC (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction CC of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In CC the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl CC migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the CC reductase reaction, this 2-ketoacid undergoes a metal-dependent CC reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. CC {ECO:0000256|HAMAP-Rule:MF_00435}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2- CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00435}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2- CC ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00435}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-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. CC {ECO:0000256|ARBA:ARBA00004885, ECO:0000256|HAMAP-Rule:MF_00435}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864, ECO:0000256|HAMAP- CC Rule:MF_00435}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|HAMAP-Rule:MF_00435, CC ECO:0000256|PROSITE-ProRule:PRU01198}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RHT56989.1}. 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; QUJF01000008; RHT56989.1; -; Genomic_DNA. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000286445; Unassembled WGS sequence. 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|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00435}; KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304, KW ECO:0000256|HAMAP-Rule:MF_00435}; Isomerase {ECO:0000313|EMBL:RHT56989.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00435}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00435}; NADP {ECO:0000256|HAMAP-Rule:MF_00435}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198}. FT DOMAIN 2..182 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000259|PROSITE:PS51850" FT DOMAIN 183..329 FT /note="KARI C-terminal knotted" FT /evidence="ECO:0000259|PROSITE:PS51851" FT NP_BIND 25..28 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT ACT_SITE 108 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT METAL 191 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 191 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 195 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 227 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 231 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 48 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 51 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 134 FT /note="NADP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 252 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" SQ SEQUENCE 331 AA; 36077 MW; B94EA18E54DE36FC CRC64; MVKMFYDADC NLSLLDGKTV AIIGFGSQGH AHAMNLKDSG VHVVVGLRPG SKHEKKAKDY GLEVMTPAEA AAAGDIIMML TPDEKQADIY KDVIAPNLKP GNVLAFAHGF NIHFKQIVPP ADVDVIMIAP KGPGHTVRSQ YLEGHGVPDL VCVEQDASGK AMDIALAYAC GIGGGRAGIL ESTFKTETET DLFGEQAVLC GGVCELMKAG FETLVEAGYA PENAYFECVH EMKLIVDLIN EGGFAKMRYS ISDTAEYGDY RTGKRIITEE TRKEMKKILR EIQDGTFASE WIQENRAGGR AHFLANRALE ADTQLEETGK KLRGMMSWLK K //