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Database: UniProt
Entry: A9BTY0_DELAS
LinkDB: A9BTY0_DELAS
Original site: A9BTY0_DELAS 
ID   A9BTY0_DELAS            Unreviewed;       646 AA.
AC   A9BTY0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490, ECO:0000256|HAMAP-Rule:MF_00012};
DE            Short=DAD {ECO:0000256|HAMAP-Rule:MF_00012};
DE            EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490, ECO:0000256|HAMAP-Rule:MF_00012};
GN   Name=ilvD {ECO:0000256|HAMAP-Rule:MF_00012};
GN   OrderedLocusNames=Daci_2756 {ECO:0000313|EMBL:ABX35394.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX35394.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX35394.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00029304};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC         Evidence={ECO:0000256|ARBA:ARBA00029304};
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:0000256|HAMAP-Rule:MF_00012};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00012};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis
CC       acid cofactor. {ECO:0000256|HAMAP-Rule:MF_00012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00029437, ECO:0000256|HAMAP-Rule:MF_00012}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 3/4. {ECO:0000256|ARBA:ARBA00029436, ECO:0000256|HAMAP-
CC       Rule:MF_00012}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00012}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486, ECO:0000256|HAMAP-Rule:MF_00012}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00012}.
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DR   EMBL; CP000884; ABX35394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9BTY0; -.
DR   STRING; 398578.Daci_2756; -.
DR   KEGG; dac:Daci_2756; -.
DR   eggNOG; COG0129; Bacteria.
DR   HOGENOM; CLU_014271_4_2_4; -.
DR   OMA; IIPGHVH; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000000784; 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; 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; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-RELATED; 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, ECO:0000256|HAMAP-Rule:MF_00012};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00012};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_00012};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00012};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00012};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00012};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00012};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00012}; Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT   ACT_SITE        549
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   BINDING         523
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   MOD_RES         151
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
SQ   SEQUENCE   646 AA;  69238 MW;  27713FEC9D3D54CE CRC64;
     MLCPGVGHNC HPGSRACRLL ATFDDPTMPT YRSKTSTGGR NMAGARALWR ATGMKDGDFD
     KPIIAIANSF TQFVPGHVHL KDLGQLVARE IEAAGGVAKE FNTIAVDDGI AMGHDGMLYS
     LPSRDIIADS VEYMVNAHCA DALVCISNCD KITPGMLMAA MRLNIPVIFV SGGPMEAGKT
     KLANPNTHKL EFKKLDLVDA MVIAADSNYT DEQVAQVERS ACPTCGSCSG MFTANSMNCL
     TEALGLSLPG NGTVLATHAD REELFKRAGR RIVELAREYY EQEDASVLPR SVGFKAFENA
     MTLDIAMGGS TNTILHLLAI AREAEIDFTM ADIDRLSRSV PQLCKVAPNT QKYHIEDVHR
     AGGIFAILGE LARAGKLHTD VPTVHAKTLG EGLAQWDITT TQDEAVRHFY LAGPAGIPTQ
     VAFSQNTRWP SLDLDRAEGC IRSYEHAFSK EGGLAVLTGN IALDGCVVKS AGVDESIHVF
     EGTAHVTESQ DEAVQNILDD KVKAGDIVVV RYEGPKGGPG MQEMLYPTSY IKSKGLGKEC
     ALLTDGRFSG GTSGLSIGHC SPEAAAGGAI GLVRNGDRIR IDIPNRSINV LVSDEELARR
     RAEQDAKGWK PAEPRPRKVS AALKAYAKLV MSADKGAVRD LSLLDD
//
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