ILV5_NEUCR
ID ILV5_NEUCR Reviewed; 402 AA.
AC P38674; Q7RVD5; Q8X0I9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ketol-acid reductoisomerase, mitochondrial;
DE EC=1.1.1.86;
DE AltName: Full=Acetohydroxy-acid reductoisomerase;
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
DE Flags: Precursor;
GN Name=ilv-2; ORFNames=B11H24.150, NCU03608;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1398116; DOI=10.1016/0378-1119(92)90018-k;
RA Sista H., Bowman B.;
RT "Characterization of the ilv-2 gene from Neurospora crassa encoding alpha-
RT keto-beta-hydroxylacyl reductoisomerase.";
RL Gene 120:115-118(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000305}.
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DR EMBL; M84189; AAB00797.1; -; Genomic_DNA.
DR EMBL; AL670005; CAD21284.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32099.1; -; Genomic_DNA.
DR PIR; JC1428; JC1428.
DR RefSeq; XP_961335.1; XM_956242.3.
DR AlphaFoldDB; P38674; -.
DR SMR; P38674; -.
DR STRING; 5141.EFNCRP00000003426; -.
DR PRIDE; P38674; -.
DR EnsemblFungi; EAA32099; EAA32099; NCU03608.
DR GeneID; 3877517; -.
DR KEGG; ncr:NCU03608; -.
DR VEuPathDB; FungiDB:NCU03608; -.
DR HOGENOM; CLU_033821_1_2_1; -.
DR InParanoid; P38674; -.
DR OMA; RAMFSWL; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 3.
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; IPR016207; KetolA_reductoisomerase_fun.
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; PIRSF000119; Ilv5_fungal; 1.
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; Branched-chain amino acid biosynthesis; Magnesium;
KW Metal-binding; Mitochondrion; NADP; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..402
FT /note="Ketol-acid reductoisomerase, mitochondrial"
FT /id="PRO_0000015632"
FT DOMAIN 63..252
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 253..400
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 177
FT /evidence="ECO:0000255"
FT BINDING 90..99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 114..119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 152..156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT CONFLICT 358
FT /note="T -> R (in Ref. 1; AAB00797)"
FT /evidence="ECO:0000305"
FT CONFLICT 392..393
FT /note="Missing (in Ref. 1; AAB00797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44623 MW; 246F795898D2A174 CRC64;
MAARNCTKAL RPLARQLATP AVQRRTFVAA ASAVRASVAV KAVAAPARQQ VRGVKTMDFA
GHKEEVHERA DWPAEKLLDY FKNDTLALIG YGSQGHGQGL NLRDNGLNVI VGVRKNGKSW
EDAIQDGWVP GKNLFDVDEA ISRGTIVMNL LSDAAQSETW PHIKPQITKG KTLYFSHGFS
PVFKDLTKVE VPTDVDVILV APKGSGRTVR SLFREGRGIN SSFAVYQDVT GKAKEKAVAL
GVAVGSGYLY ETTFEKEVYS DLYGERGCLM GGIHGMFLAQ YEVLRERGHS PSEAFNETVE
EATQSLYPLI GAHGMDWMFD ACSTTARRGA IDWTPKFKDA LKPVFNNLYD SVKNGDETKR
SLEYNSQPDY RERYEAELDE IRNLEIWRAG KAVRSLRPEN QK