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Entry: A0A2T3A097_9PEZI
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ID   A0A2T3A097_9PEZI        Unreviewed;       602 AA.
AC   A0A2T3A097;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE            EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN   ORFNames=BD289DRAFT_374044 {ECO:0000313|EMBL:PSR80424.1};
OS   Coniella lustricola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX   NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSR80424.1, ECO:0000313|Proteomes:UP000241462};
RN   [1] {ECO:0000313|EMBL:PSR80424.1, ECO:0000313|Proteomes:UP000241462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B22-T-1 {ECO:0000313|EMBL:PSR80424.1,
RC   ECO:0000313|Proteomes:UP000241462};
RA   Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA   Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT   "Coniella lustricola, a new species from submerged detritus.";
RL   Mycol. Prog. 17:191-203(2018).
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; KZ678531; PSR80424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3A097; -.
DR   STRING; 2025994.A0A2T3A097; -.
DR   InParanoid; A0A2T3A097; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000241462; 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   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:SF13; DIHYDROXY-ACID DEHYDRATASE; 1.
DR   PANTHER; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 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:UP000241462}.
SQ   SEQUENCE   602 AA;  64544 MW;  5D152965789B817C CRC64;
     MPGQDDYIQW PCLPPGGALN RWSHAITREH DFVAAKAMLY AAGVPDEHTM QNAPQVGIAT
     VWWEGNPCNT HLMDLGKIVK KAVEKQNMLA WQFNTIGVSD GITMGSDAMR YSLQSREIIA
     DSIETVTCAQ RHDANISLPG CDKNMPGVIM AAARHNRPFL MIYGGTIRKG HSTLLNSDVN
     ISTCLEARGA YTYGKLHAQC PKPNGDAATP ADVLDDLERH SCPSVGACGG MYTANTMATA
     IEAMGLSLPG SSSYPATSPE KARECERAAD AIKVCMERDI RPRDLLSRAA FENALVLTMV
     LGGSTNGVLH FLAMANSADV ALTLDDIDRA SNRTPFLADL QPSGRHMMED LYDIGGTPSV
     LKMLIAAGLI DGSLMTVTGK TLAENCASWP SLDPGQKIIR PLDDPIKKTG HLRVLRGNLA
     PQGAVAKITG KEGLSFTGKA RVFDKEHELD AALQRGDIKP EHGNLVLVVR YEGPRGGPGM
     PEQLTASAAI IGAGLKTVAL ITDGRYSGAS HGFIVGHICP EAAVGGPIAL VKDGDEIRID
     ATENRIDILN VDLDELRERK KSWRPPVTKP LRGTLAKYAR LVGDASHGAV TDLAEPLEST
     NW
//
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