(data stored in ACNUC6288 zone)

SWISSPROT: Q6BLZ4_DEBHA

ID   Q6BLZ4_DEBHA            Unreviewed;       399 AA.
AC   Q6BLZ4;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Ketol-acid reductoisomerase, mitochondrial {ECO:0000256|PIRNR:PIRNR000119};
DE            EC=1.1.1.86 {ECO:0000256|PIRNR:PIRNR000119};
DE   AltName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000256|PIRNR:PIRNR000119};
DE   AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|PIRNR:PIRNR000119};
GN   OrderedLocusNames=DEHA2F09570g {ECO:0000313|EMBL:CAG89118.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89118.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89118.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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|PIRNR:PIRNR000119};
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|PIRNR:PIRNR000119};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000119};
CC       Note=Binds 2 magnesium ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000119};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion
CC       {ECO:0000256|PIRNR:PIRNR000119}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE-
CC       ProRule:PRU01198}.
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DR   EMBL; CR382138; CAG89118.1; -; Genomic_DNA.
DR   RefSeq; XP_460777.1; XM_460777.1.
DR   STRING; 4959.XP_460777.1; -.
DR   EnsemblFungi; CAG89118; CAG89118; DEHA2F09570g.
DR   GeneID; 2903619; -.
DR   KEGG; dha:DEHA2F09570g; -.
DR   HOGENOM; HOG000016231; -.
DR   InParanoid; Q6BLZ4; -.
DR   KO; K00053; -.
DR   OMA; RAMFSWL; -.
DR   OrthoDB; 720924at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal 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; 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;
DR   PRODOM; Q6BLZ4.
DR   SWISS-2DPAGE; Q6BLZ4.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000119,
KW   ECO:0000256|PROSITE-ProRule:PRU01198};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR000119,
KW   ECO:0000256|PROSITE-ProRule:PRU01198};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE-
KW   ProRule:PRU01198};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE-
KW   ProRule:PRU01198}; Mitochondrion {ECO:0000256|PIRNR:PIRNR000119};
KW   NADP {ECO:0000256|PIRNR:PIRNR000119};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000119, ECO:0000256|PROSITE-
KW   ProRule:PRU01198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN       60    250       KARI N-terminal Rossmann.
FT                                {ECO:0000259|PROSITE:PS51850}.
FT   DOMAIN      251    398       KARI C-terminal knotted.
FT                                {ECO:0000259|PROSITE:PS51851}.
FT   METAL       259    259       Magnesium 1. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01198}.
FT   METAL       259    259       Magnesium 2. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01198}.
FT   METAL       263    263       Magnesium 1. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01198}.
FT   METAL       295    295       Magnesium 2. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01198}.
FT   METAL       299    299       Magnesium 2. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01198}.
FT   BINDING     321    321       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
SQ   SEQUENCE   399 AA;  44352 MW;  53D67F203BD09113 CRC64;
     MSIRNASIRM ARMASNNAAK QVASKRALSA LANAARPVVA RKSIAPAAAR GVKTINFGGM
     DEIVHERADW PREKLLEYFK NDTLALIGYG SQGYGQGLNL RDNGLNVIIG VRKDGASWKA
     AIEDGWVPGE NLFDVNEAIG KGTYIMNLLS DAAQSETWES IKPQLTEGKT LYFSHGFSPV
     FKELTHVEPP TNIDVILAAP KGSGRTVRTL FKEGRGINSS YAVWNDVTGK AEEKAIALAV
     AIGSGYVYQT TFEREVNSDL YGERGCLMGG IHGMFLAQYE VLRENGHTPS EAFNETVEEA
     TQSLYPLIGK YGMDYMYDAC STTARRGALD WYPRFKDALK PVFNDLYESV KNGTETQRSL
     DFNSQSDYRA RLEEELETIR SMEIWRVGKE VRKLRPENQ
//

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