ID E3HNS0_ACHXA Unreviewed; 580 AA.
AC E3HNS0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=AXYL_03789 {ECO:0000313|EMBL:ADP17109.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP17109.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP17109.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP17109.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002287; ADP17109.1; -; Genomic_DNA.
DR RefSeq; WP_013394423.1; NC_014640.1.
DR AlphaFoldDB; E3HNS0; -.
DR STRING; 762376.AXYL_03789; -.
DR KEGG; axy:AXYL_03789; -.
DR PATRIC; fig|762376.5.peg.3802; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_4_2_4; -.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000006876; 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 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, 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}.
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 127
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 448
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT MOD_RES 127
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
SQ SEQUENCE 580 AA; 60177 MW; FA55E698FA238168 CRC64;
MKDLHKHRSR TVTEGVTRAP HRAFLRATGL DDEAIDKPFV AIVDTYGENT PCSMSLNQIS
DNVRLGIAAG GGVPIRGSAI SVSDGTSMNH SGMRFSLVSR ETIADSVELF VRAHCYDALV
GVAGCDKTLP GILMGMVRVN VPGVFLFGGA MLPGVAPDGS QATILTAIEA VGAAQRGDMS
AETLRGIEKR CTPTAGSCPG QFTANTMAMV AEVLGLAPLG SAMVPAVYSE RIAIARRAGE
SVMRTLRNGG PLPRDLVTRK SLENACAAVA ATGGSTNAML HIPAIAHEAG IAFTLDDVSD
VLARTPLIGD MQPGGRYLAV DLHHVGGVPA VLNALLAGGH IHGDTLTQSG ETLETALRAF
PGPDGRVVKP HDEPLSPNAG LVVLRGNLAP DGAALKTAGL KQLVFSGTAR VFETEEDCMA
VVAAGAYREG DVLVIRNEGP KGGPGMREML SVTAAIYGQG MGEKVALLTD GRFSGATRGM
CIGYVGPEAA AGGPIRLLRD GDRIHIDAIK GSLDVELPDE ELAERAKASQ PFVRGRLGGV
LEKYEALVRP AKLGAVTHSG AVTWPYEASL GETPAQGGQQ
//
