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Database: UniProt
Entry: A0A411WGD3_9GAMM
LinkDB: A0A411WGD3_9GAMM
Original site: A0A411WGD3_9GAMM 
ID   A0A411WGD3_9GAMM        Unreviewed;       492 AA.
AC   A0A411WGD3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
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:QBH95094.1};
GN   ORFNames=EKN56_00885 {ECO:0000313|EMBL:QBH95094.1};
OS   Jinshanibacter zhutongyuii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Jinshanibacter.
OX   NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH95094.1, ECO:0000313|Proteomes:UP000293154};
RN   [1] {ECO:0000313|EMBL:QBH95094.1, ECO:0000313|Proteomes:UP000293154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF-458 {ECO:0000313|EMBL:QBH95094.1,
RC   ECO:0000313|Proteomes:UP000293154};
RA   Ge Y.;
RT   "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL   Submitted (MAR-2019) 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}.
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DR   EMBL; CP034752; QBH95094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411WGD3; -.
DR   KEGG; prag:EKN56_00885; -.
DR   OrthoDB; 9804088at2; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000293154; 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: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:QBH95094.1};
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..344
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;  53759 MW;  0E5A644AAEF9FCAC CRC64;
     MANYFNTLNL RQQLAQLGQC RFMGRDEFAD ESGFLKGKKI VIVGCGAQGL NQGLNMRDSG
     LDIAYALRKE AIDEKRASWR KATENGFKVG TYEELIPQAD LVVNLTPDKQ HSAVVQAVQP
     LMKQGAALGY SHGFNIVEVG ETIRPDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
     NDPKGEGMAI AKAWAAATGG HRAGVLQSSF VAEVKSDLMG EQTILCGMLQ AGSILCFDKL
     VADGASPAYA EKLVQYGWET TTEALKQGGI TLMMDRLSNS AKLRAFALSE QLKALMAPLF
     QKHMDDIISG AFSEGMMADW ANNDAKLLGW REETGRTAFE NAPQQEGKIS EQEYFDHGVL
     MIAMVKAGVE LAFETMVVSG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG
     NYLFSNAAVP LLREKFMGSL QAGDLGKSVA AAEIDNAQLR DVNEAIRNHP IEVIGKKLRG
     YMTDMKRIAV AG
//
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