ILVD_PSEPF
ID ILVD_PSEPF Reviewed; 613 AA.
AC Q3K559;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012};
DE Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012};
DE EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012};
GN Name=ilvD {ECO:0000255|HAMAP-Rule:MF_00012}; OrderedLocusNames=Pfl01_5358;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Functions in the biosynthesis of branched-chain amino acids.
CC Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate
CC (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-
CC 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-
CC dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate),
CC the penultimate precursor to L-isoleucine and L-valine, respectively.
CC {ECO:0000255|HAMAP-Rule:MF_00012}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00012};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-
CC oxopentanoate + H2O; Xref=Rhea:RHEA:27694, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35146, ChEBI:CHEBI:49258; EC=4.2.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis
CC acid cofactor. {ECO:0000255|HAMAP-Rule:MF_00012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-
CC Rule:MF_00012}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC Rule:MF_00012}.
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DR EMBL; CP000094; ABA77095.1; -; Genomic_DNA.
DR RefSeq; WP_011336405.1; NC_007492.2.
DR AlphaFoldDB; Q3K559; -.
DR SMR; Q3K559; -.
DR STRING; 205922.Pfl01_5358; -.
DR PRIDE; Q3K559; -.
DR EnsemblBacteria; ABA77095; ABA77095; Pfl01_5358.
DR KEGG; pfo:Pfl01_5358; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_4_2_6; -.
DR OMA; TQGRNMA; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000002704; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.30.80; -; 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 Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; SSF143975; 1.
DR TIGRFAMs; TIGR00110; ilvD; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..613
FT /note="Dihydroxy-acid dehydratase"
FT /id="PRO_0000225411"
FT ACT_SITE 515
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT BINDING 122
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT BINDING 193
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT MOD_RES 124
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
SQ SEQUENCE 613 AA; 65874 MW; CCC973067C322E29 CRC64;
MPDYRSKTST HGRNMAGARA LWRATGMKDD DFKKPIIAIA NSFTQFVPGH VHLKDLGQLV
AREIERAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSREII ADSVEYMVNA HCADAIVCIS
NCDKITPGML MAALRLNIPV IFVSGGPMEA GKTKLASHGL DLVDAMVIAA DSSASDEKVA
EYERSACPTC GSCSGMFTAN SMNCLTEALG LALPGNGSTL ATHSDREQLF LQAGRTIVEL
CKRYYGENDE SVLPRNIANF KAFENAMMLD IAMGGSTNTI LHLLAAAQEA EIDFDLRDID
RLSRKVPQLC KVAPNIQKYH MEDVHRAGGI FSILGSLARG GLLHTDLPTV HSRSMEEAIA
KWDITQTDDE AVHHFFKAGP AGIPTQTAFS QSTRWETLDD DRENGCIRSF EHAYSKEGGL
AVLYGNIALD GCVVKTAGVD ESIHVFEGNA KIFESQDSAV RGILADEVKE GDIVIIRYEG
PKGGPGMQEM LYPTSYLKSK GLGKACALLT DGRFSGGTSG LSIGHASPEA AAGGAIGLVQ
DGDKVLIDIP NRSINLLISD EELAARRVEQ DKKGWKPVEQ RPRKVTTALK AYALLATSAD
KGAVRNKAML DGL
