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Database: UniProt
Entry: A0A1I2WTA4_9FIRM
LinkDB: A0A1I2WTA4_9FIRM
Original site: A0A1I2WTA4_9FIRM 
ID   A0A1I2WTA4_9FIRM        Unreviewed;       556 AA.
AC   A0A1I2WTA4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ORFNames=SAMN05660649_03612 {ECO:0000313|EMBL:SFH03927.1};
OS   Desulfotruncus arcticus DSM 17038.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfotruncus.
OX   NCBI_TaxID=1121424 {ECO:0000313|EMBL:SFH03927.1, ECO:0000313|Proteomes:UP000199337};
RN   [1] {ECO:0000313|Proteomes:UP000199337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17038 {ECO:0000313|Proteomes:UP000199337};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOOX01000014; SFH03927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2WTA4; -.
DR   STRING; 341036.SAMN05660649_03612; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000199337; Unassembled WGS sequence.
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:UP000199337}.
FT   ACT_SITE        468
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   BINDING         121
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         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   MOD_RES         121
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
SQ   SEQUENCE   556 AA;  58924 MW;  189EB14FEC5A4394 CRC64;
     MRSDAMKKGL DKAPHRSLFN ALGLTRQELE RPMIGVVNSF NEIVPGHMHL REITEAVKAG
     VRMNGGTPFE FPAIAVCDGI AMNHSGMKYS LASRELIADS VEVMSMAHPF DGIVLVTSCD
     KVVPGMLMAA ARLDIPAIVV SGGPMMAGRL NGKDLSLSNI FEGVGSVRAG TMTEEELALY
     EESVCPGCGS CAGMFTANSM NCLTEVLGMA LPGNGTLPAV SAARRRLAKL SGMRVVDLVR
     ENLKPSDILT EKAFANGLAM DMALGCSTNT VLHLPAIASE ADIKIELDQI NRISEKTPNL
     CKLSPAGPHY MQDLNEAGGI SAVLRELSEH GFIDGSTLTV TGRTLGENVA AASVLRREVI
     RSVEEPYSST GGIAILYGNL APGGAVVKRS AVAPEMLQHR GPARVFNSEE EAVQALNNLE
     IQKGDVIIIR YEGPKGGPGM REMLTPTATV AGLGLDKDVA LITDGRFSGA TRGASIGHAT
     PEAAEGGPIA ALQDGDIIDI NIPECKLNVL LSDEELAARM NRWVKPEPRV RKGYLVRYAK
     LVTSAGTGAV LKKDFE
//
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