ID A0A417GL56_9CLOT Unreviewed; 331 AA. AC A0A417GL56; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. 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; Clostridiales; Clostridiaceae; OC Butyricicoccus. OX NCBI_TaxID=2292295 {ECO:0000313|EMBL:RHT56989.1}; RN [1] {ECO:0000313|EMBL:RHT56989.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AM29-23AC {ECO:0000313|EMBL:RHT56989.1}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut RT microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 Isomerase {ECO:0000313|EMBL:RHT56989.1}; 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:RHT56989.1}. FT DOMAIN 2 182 KARI N-terminal Rossmann. FT {ECO:0000259|PROSITE:PS51850}. FT DOMAIN 183 329 KARI C-terminal knotted. FT {ECO:0000259|PROSITE:PS51851}. FT NP_BIND 25 28 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}. FT ACT_SITE 108 108 {ECO:0000256|HAMAP-Rule:MF_00435}. FT METAL 191 191 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 191 191 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 195 195 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 227 227 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 231 231 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT BINDING 48 48 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}. FT BINDING 51 51 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}. FT BINDING 134 134 NADP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00435}. FT BINDING 252 252 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT 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 //