ID   ILVD_ACTPJ              Reviewed;         611 AA.
AC   B0BS03;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 91.
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};
GN   OrderedLocusNames=APJL_0097;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA   Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA   Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA   Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(2008).
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000687; ABY68703.1; -; Genomic_DNA.
DR   RefSeq; WP_005600080.1; NC_010278.1.
DR   AlphaFoldDB; B0BS03; -.
DR   SMR; B0BS03; -.
DR   KEGG; apj:APJL_0097; -.
DR   HOGENOM; CLU_014271_4_2_6; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.50.30.80:FF:000001; Dihydroxy-acid dehydratase; 1.
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; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR056740; ILV_EDD_C.
DR   InterPro; IPR000581; ILV_EDD_N.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   NCBIfam; TIGR00110; ilvD; 1.
DR   NCBIfam; NF009103; PRK12448.1; 1.
DR   PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-RELATED; 1.
DR   Pfam; PF24877; ILV_EDD_C; 1.
DR   Pfam; PF00920; ILVD_EDD_N; 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; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..611
FT                   /note="Dihydroxy-acid dehydratase"
FT                   /id="PRO_1000089364"
FT   ACT_SITE        517
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         195
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   BINDING         491
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   611 AA;  65408 MW;  7BEBD1C51958AEB9 CRC64;
     MPILRSATST QGRNMAGARA LWRATGMKEN DFGKPIIAVV NSFTQFVPGH VHLRDMGKLV
     AEQIEAAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRDLI ADSVEYMVNA HCADAMVCIS
     NCDKITPGML MAAMRLNIPA VFVSGGPMEA GKTKLSNQLI KLDLVDAMMK SADKTVCDDD
     VDAIEKSACP TCGSCSGMFT ANSMNCLTEA LGLSLPGNGS MLATHADRKE LFLTAGRQIV
     ELCKRYYEQD DASVLPRSIA TKAAFENAMS LDIAMGGSTN TVLHLLAAAQ EAEVDFTMAD
     IDRLSRKVPC LSKVAPNTNK YHMEDVHRAG GIMAILGELE RADLLHSDTR TVLGMTIGEQ
     IAKYDITLTK DEAVHKFFRA GPAGIRTTKA FSQDCRWDTV DDDRQNGCIR SKEFAYSQDG
     GLAMLTGNIA LDGCIVKTAG VDESILKFTG DAIVFESQEE AVEGILGGKV RAGHVVIIRY
     EGPKGGPGMQ EMLYPTTYLK SIGLGKECAL LTDGRFSGGT SGLSIGHCSP EAASGGTIGL
     VRDGDKIAID IPNRSIQLLV SDEELAVRRA EQDAKGWKPA NRQREVSMAL KMFGHFATSA
     DKGAVRDKTK L
//