ID A0A1Z5JQZ0_FISSO Unreviewed; 636 AA.
AC A0A1Z5JQZ0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN ORFNames=FisN_27Lh073 {ECO:0000313|EMBL:GAX16359.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX16359.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX16359.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX16359.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
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:GAX16359.1}.
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DR EMBL; BDSP01000104; GAX16359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5JQZ0; -.
DR InParanoid; A0A1Z5JQZ0; -.
DR OrthoDB; 238at2759; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000198406; 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:UniProtKB-EC.
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, ECO:0000313|EMBL:GAX16359.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..636
FT /note="dihydroxy-acid dehydratase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013074544"
SQ SEQUENCE 636 AA; 68294 MW; 148946B22A6B9A3C CRC64;
MKFVLFLSLT GAAHGFAPVQ SGTRSSTALF MSEEGPILNK WSRTLTQTKV QGASQAMLYA
TGLTQQDMNK PQVGIASVWY EGNPCNMHLL DLSEKVKRGV EQANCVGFRF NTVGVSDGIS
MGTSGMRYSL QSRDLIADSM ETTMSGQWYD GLIALPGCDK NMPGCIMAMG RLNRPGIMVY
GGTIRAGKQP STGQPLDIVS AFQSYGQYVY DKISEEERQE IIQHSCPGPG ACGGMYTANT
MATAIEALGM SLPYSSSSPA DSKEKADECF QAGAAMRKLL EMDLKPRDIM TKEAFENAIR
MIMITGGSTN AVLHLVAMSR STQNPSAYIT LEDFQRISDQ TPFLADLKPS GKYVMEDVQN
IGGTPGLLRF MLDEGFLDGS QMTVTGYSHA ENLANHPGLK PGQDIIRPLS DPIKATGHLL
MMYGNLCPGG GVAKITGKEG ETFTGTARVY DNEPSMMRGL ENKEIVPGDV VIIRYEGPKG
GPGLPEMLTP TSAIMGAGLG DKVALLTDGR FSGGSHGFCI GHITPEAQVG GPLALVKTGD
PIRIDARPSQ RTIDLLISDE EWEKRRREWV PPPLRATQGT LFRYIQTVAT ASEGCVTDEI
GTQSVTSIVA AAPKTPAVAE LEAKIAQLEA QLGIRS
//
