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Database: UniProt
Entry: A0A0C9YRN2_9AGAM
LinkDB: A0A0C9YRN2_9AGAM
Original site: A0A0C9YRN2_9AGAM 
ID   A0A0C9YRN2_9AGAM        Unreviewed;       589 AA.
AC   A0A0C9YRN2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE            EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN   ORFNames=PISMIDRAFT_166069 {ECO:0000313|EMBL:KIK27710.1};
OS   Pisolithus microcarpus 441.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK27710.1, ECO:0000313|Proteomes:UP000054018};
RN   [1] {ECO:0000313|EMBL:KIK27710.1, ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|EMBL:KIK27710.1,
RC   ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
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 = 3-methyl-2-oxobutanoate
CC         + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:49072; EC=4.2.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00029304};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC         Evidence={ECO:0000256|ARBA:ARBA00029304};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00029437}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 3/4. {ECO:0000256|ARBA:ARBA00029436}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
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DR   EMBL; KN833695; KIK27710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9YRN2; -.
DR   STRING; 765257.A0A0C9YRN2; -.
DR   HOGENOM; CLU_014271_4_2_1; -.
DR   OrthoDB; 238at2759; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000054018; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR   HAMAP; MF_00012; IlvD; 1.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR004404; DihydroxyA_deHydtase.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   NCBIfam; TIGR00110; ilvD; 1.
DR   PANTHER; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 1.
DR   PANTHER; PTHR21000:SF5; DIHYDROXY-ACID DEHYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
DR   PROSITE; PS00887; ILVD_EDD_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054018}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   589 AA;  63620 MW;  B88658602E8092C6 CRC64;
     MSSVEIHSVS RPSRGSPNDR LNKISCQLTQ NKARGGAQAM LYATGLTEED MDKPQIGISP
     IWWEGNPCNF HLLDLARKVK EGCKEEGLVG LIFNTIGISD AITMGTDGMR YSLPSRDLIA
     DSIEAVTMAQ YYDGNIAIPG CDKNMPGVVM AAVRHNRPTI VVYGGTIGVG TRHLDCPSMG
     FKKGGPVNIS DAFESYGAYT VGLINDEERL DVVRHACPGP GACGGMYTAN TMGAVLEVLG
     MSLPYSSSTP AMYPEKSQEC FKAAKYLKRL LELDLKPKDI LTRWSFLNAI TIVNIIGGST
     NAVLHLLAMA RAADIPLTID DFQEISDRTP YIADLKPSGK YYMEDVHKIG GIPALLKYLL
     KYTNLIDGNQ MTVTGKTLAE NLEDVAELDF GSQDVIRRIE DPIKTTGHVT ILRGTLAPGT
     AVAKLTGKEG LHFEGIAKCF DKESDFYPSL EKGEIKPGTV LIFRYQGPRG APGMPEMLGP
     TGALMGAGLG NTTALVTDGR FSGASRGFII GHVVPEAVLG GPIALVKDGD RILIDADSRT
     IDWVIDESEK LSRRKEWEAS GKSGLNVRRG VLYRYARDVA PASEGAYCD
//
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