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Database: UniProt
Entry: A0A1Q5TWY5_9GAMM
LinkDB: A0A1Q5TWY5_9GAMM
Original site: A0A1Q5TWY5_9GAMM 
ID   A0A1Q5TWY5_9GAMM        Unreviewed;       492 AA.
AC   A0A1Q5TWY5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=Xentx_02653 {ECO:0000313|EMBL:OKP04726.1};
OS   Xenorhabdus thuongxuanensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1873484 {ECO:0000313|EMBL:OKP04726.1, ECO:0000313|Proteomes:UP000186277};
RN   [1] {ECO:0000313|EMBL:OKP04726.1, ECO:0000313|Proteomes:UP000186277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30TX1 {ECO:0000313|EMBL:OKP04726.1,
RC   ECO:0000313|Proteomes:UP000186277};
RA   Kaempfer P., Tobias N.J., Phan Ke L., Bode H.B., Glaeser S.P.;
RT   "Xenorhabdus thuongxuanensis sp. nov. and Xenorhabdus eapokensis sp. nov.,
RT   isolated from Steinernema species.";
RL   Submitted (SEP-2016) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000507, 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|PROSITE-ProRule:PRU01198}.
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:OKP04726.1}.
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DR   EMBL; MKGR01000020; OKP04726.1; -; Genomic_DNA.
DR   RefSeq; WP_074020686.1; NZ_MKGR01000020.1.
DR   AlphaFoldDB; A0A1Q5TWY5; -.
DR   OrthoDB; 9804088at2; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000186277; 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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00435; IlvC; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013023; KARI.
DR   InterPro; IPR000506; KARI_C.
DR   InterPro; IPR013116; KARI_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00465; ilvC; 1.
DR   PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01450; IlvC; 2.
DR   Pfam; PF07991; IlvN; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51851; KARI_C; 2.
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:OKP04726.1};
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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00435}.
FT   DOMAIN          15..208
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          209..340
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   DOMAIN          345..485
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         45..48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         68
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         76
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         108..110
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         389
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         393
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
SQ   SEQUENCE   492 AA;  54345 MW;  88D40E7F6372636A CRC64;
     MANYFDTLNL RQQLAQLGKC RFMAREEFAD EAGYLKGKKV VIIGCGAQGL NQGLNMRDSG
     LDIAYALRKE AIDEKRPSWR KATENGFKVG TYEELIPQAD LVINLTPDKQ HSTVVQAVQP
     LMKEGAALGY SHGFNIVEVG EPIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
     NDAKGEGMAI AKAWAAATGG HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCYDQL
     VADGVDPGYA GKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKTILTPLF
     QKHMDDIISG EFSSTMMADW ANDDKNLLTW REETGKTPFE NYPDCTGHIS EQEYFDHGVL
     MVAMVKAGVE LAFETMVDTG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG
     NYLFSYIAVP LLKEKFMATL QSGDLGKEVA DRSVDNAQLR DVNEAIRNHP IEIIGRTLRG
     YMTDMKRIAV GG
//
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