ID A0A421GNK1_9STRA Unreviewed; 596 AA.
AC A0A421GNK1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN ORFNames=BBI17_005797 {ECO:0000313|EMBL:RLN31475.1}, BBO99_00005452
GN {ECO:0000313|EMBL:RLN79190.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN79190.1, ECO:0000313|Proteomes:UP000285624};
RN [1] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN31475.1}, and Chile4
RC {ECO:0000313|EMBL:RLN79190.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLN79190.1}.
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DR EMBL; MAYM02000969; RLN31475.1; -; Genomic_DNA.
DR EMBL; MBDN02000157; RLN79190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421GNK1; -.
DR STRING; 325452.A0A421GNK1; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; 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:UP000285624}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 63612 MW; 8AFF3E83486BDA76 CRC64;
MLSKTMRSAT SPMRKTLTHR TFSSVSNDSD IPKAVDGVRI NRYSANVTQP KARGASQAML
YATGMTEEDM DKPQVGIASM WWEGNPCNMH LLDLAGEVKK GVNAAGLVGL RFNTIGVSDG
ISMGTDGMSY SLQSRDLIAD SVETVMGGQW YDANICIPGC DKNMPGCVIA MARVNRPSLM
VYGGTIRAGC SSKGETLDIV SAFQAYGEYI AGRITEEERH DIIRHACPGA GACGGMYTAN
TMATAIETLG LSLPFSSSFP ADSPEKQTEC ITAGEAIKVL LEKDIKPLDI LCREAFDNAI
TVTMALGGST NAVLHLIAIA RAAGIPLTID DFEKISERVP FLADLKPSGK FVMEDIHRVG
GTPAVLKYLM NQGFINGDCL TVTGKTLGEN LKNVPDLSDN HEIIYPVDRP LKSSGHLRIL
RGDLAPEGSV AKITGKEGLV FTGTAKVYDC EEDMMAGLER NEITKGSVVI IRYEGPKGGP
GMPEMLAPTS AIMGAGLGKD VAMLTDGRFS GGSHGFIIGH ITPEAQVGGP IALVKDGDKI
TVDAENNRID FIDVSADELV QRKKEWVAPP LKATRGTLHK FIKNVKSASE GCVTDE
//
