GenomeNet

Database: UniProt
Entry: A0A0C9ZJ13_9AGAM
LinkDB: A0A0C9ZJ13_9AGAM
Original site: A0A0C9ZJ13_9AGAM 
ID   A0A0C9ZJ13_9AGAM        Unreviewed;       409 AA.
AC   A0A0C9ZJ13;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=CY34DRAFT_459546 {ECO:0000313|EMBL:KIK37420.1};
OS   Suillus luteus UH-Slu-Lm8-n1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX   NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK37420.1, ECO:0000313|Proteomes:UP000054485};
RN   [1] {ECO:0000313|EMBL:KIK37420.1, ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK37420.1,
RC   ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RA   Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA   Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA   LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA   Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR000119};
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|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   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004885}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR000119}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PIRNR:PIRNR000119,
CC       ECO:0000256|PROSITE-ProRule:PRU01198}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN835452; KIK37420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9ZJ13; -.
DR   STRING; 930992.A0A0C9ZJ13; -.
DR   HOGENOM; CLU_033821_1_2_1; -.
DR   InParanoid; A0A0C9ZJ13; -.
DR   OrthoDB; 1090117at2759; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000054485; Unassembled WGS sequence.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR016207; KetolA_reductoisomerase_fun.
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; PIRSF000119; Ilv5_fungal; 1.
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,
KW   ECO:0000256|PIRNR:PIRNR000119};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|PIRNR:PIRNR000119};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000119};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000119};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000119};
KW   NADP {ECO:0000256|PIRNR:PIRNR000119};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054485}.
FT   DOMAIN          69..258
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          259..406
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ   SEQUENCE   409 AA;  44865 MW;  00F2D8432DAFD968 CRC64;
     MASIASRSAS ALRAASRRAP RAGAKIAVKP AQSASYSLLA RQALAGTSRK PAFQSAARGV
     KTLNFAGTEE VVYERSDWPL AKLQDYFKND TLALIGYGSQ GHGQGLNARD NGLNVIVGVR
     KDGESWRQAM EDGWVPGETL FPIEDAINRG TIIMNLLSDA AQSQTWSTVA PLITKGKTLY
     FSHGFSVVYK EDTKVIPPKD VDVILVAPKG SGRTVRTLFK EGRGINSSVA VFQDVTGQAM
     EKAVALGVAV GSGYMYETTF EKEVYSDLYG ERGVLMGAIQ GLFCAQYKVL RANGHSPSEA
     FNETVEEATQ SLYPLIGQKG MDYMYNACST TARRGALDWA PIFEKTNTPI FEQLYESVRN
     GTETRKSLEF NGRSTYRQDL AKELKEIDDQ EIWRAGKTVR SLRPDYKAE
//
DBGET integrated database retrieval system