ID S3CX89_GLAL2 Unreviewed; 606 AA.
AC S3CX89;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN ORFNames=GLAREA_00709 {ECO:0000313|EMBL:EPE29549.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE29549.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE29549.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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; KE145367; EPE29549.1; -; Genomic_DNA.
DR RefSeq; XP_008083658.1; XM_008085467.1.
DR AlphaFoldDB; S3CX89; -.
DR STRING; 1116229.S3CX89; -.
DR GeneID; 19459767; -.
DR KEGG; glz:GLAREA_00709; -.
DR eggNOG; KOG2448; Eukaryota.
DR HOGENOM; CLU_014271_4_1_1; -.
DR OMA; YLMEDLY; -.
DR OrthoDB; 238at2759; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000016922; 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:UP000016922}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 64587 MW; D5CED45320A52CD0 CRC64;
MEPSNYTDIP DEPRYISFPS VEPGTKTSDG KQVLNRWSST ITREHDFPGA QAMLYAAGIP
DRMSMKTSPH VGISSVWWEG NPCNMHLNDL GKIVKQAVQK QGMLAWQFNT IGVSDAITMG
GEGMRFSLQT REIIADSIET VTCAQHHDAN ISIPGCDKNM PGVIMAAARH NRPFLMIYGG
SIKKGHSKLL NKNVNISTCY EAAGAFAYNR LQPTEEYANK GCTASDVMED LERHACPGAG
ACGGMYTANT MSTAIEAMGL CLPGSSSNPA ESPAKMRECE NAAEAIRICM EKNIRPRDLL
TKESFENALV ITMALGGSTN GVLHFLAMAG TAEVPLTLDD VQRVSDKIPF LADLAPSGKF
LMEDLFEIGG TPSVLKLLVA AGLINGNIPT VTGKTLAENI EPFPSLPADQ KIIRPLSNPI
KKTGHLQILR GNLSPGGAVA KITGKEGLTF TGKARVFNKE HELDNALTKG QIPHGENLVL
IVRYEGPKGG PGMPEQLKSS AAIMGAGLTN VALVTDGRYS GASHGFIVGH VVPEAAVGGP
IAIVQDGDIV TISAETNTLS MHVSDDEIAA RMKAWKPPKS VVNRGVLAKY AKLVGDASHG
AMTDLF
//
