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Database: UniProt
Entry: I3ECR4_BACMM
LinkDB: I3ECR4_BACMM
Original site: I3ECR4_BACMM 
ID   I3ECR4_BACMM            Unreviewed;       340 AA.
AC   I3ECR4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
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:AIE60944.1};
GN   ORFNames=BMMGA3_12755 {ECO:0000313|EMBL:AIE60944.1};
OS   Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE60944.1, ECO:0000313|Proteomes:UP000027602};
RN   [1] {ECO:0000313|EMBL:AIE60944.1, ECO:0000313|Proteomes:UP000027602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGA3 / ATCC 53907 {ECO:0000313|Proteomes:UP000027602};
RX   PubMed=25758049;
RA   Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT   "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT   methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT   previously uncharted transcriptional landscape.";
RL   BMC Genomics 16:73-73(2015).
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}.
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DR   EMBL; CP007739; AIE60944.1; -; Genomic_DNA.
DR   RefSeq; WP_003347570.1; NZ_CP007739.1.
DR   AlphaFoldDB; I3ECR4; -.
DR   STRING; 796606.BMMGA3_12755; -.
DR   KEGG; bmet:BMMGA3_12755; -.
DR   eggNOG; COG0059; Bacteria.
DR   HOGENOM; CLU_033821_0_1_9; -.
DR   OrthoDB; 9804088at2; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000027602; 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   Gene3D; 6.10.240.10; -; 1.
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; 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   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; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000116; IlvC_gammaproteo; 2.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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:AIE60944.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000027602}.
FT   DOMAIN          2..180
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          181..326
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         25..28
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         52
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         132
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         189
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         189
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         193
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         225
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         229
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         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
SQ   SEQUENCE   340 AA;  37632 MW;  042FDA353FCDE0C3 CRC64;
     MAKMYYNGDA NEQYLNGKKV AVIGYGSQGH AHAQNMRDSG VDVVIGLRKG KSWEKAEQDG
     FKVYSVGEAT AQADVVMILL PDELQPKVYK EEIEPNLTNQ ALMFAHGFNI HFNQIVPPKE
     CDVLLVAPKG PGHLVRRTYQ EGAGVPALFA IYQDVSGEAK ELALAYAKAI GSLRAGALET
     TFKEETETDL FGEQAVLCGG LTALVKAGFE TLTEAGYQPE LAYFECLHEL KLIVDLMYEG
     GLAGMRYSIS DTAQWGDFVS GPRVINDQVK QEMKAVLKDI QEGKFAKGWI LENQANRPVF
     NAINEREKEH PIEKVGRELR KMMPFVNKDK KKEVVASAKN
//
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