ILVD_RHILW
ID ILVD_RHILW Reviewed; 612 AA.
AC B5ZZ62;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Rleg2_1361;
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304;
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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}.
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; CP001191; ACI54655.1; -; Genomic_DNA.
DR RefSeq; WP_012557371.1; NC_011369.1.
DR AlphaFoldDB; B5ZZ62; -.
DR SMR; B5ZZ62; -.
DR STRING; 395492.Rleg2_1361; -.
DR EnsemblBacteria; ACI54655; ACI54655; Rleg2_1361.
DR KEGG; rlt:Rleg2_1361; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_4_2_5; -.
DR OMA; TQGRNMA; -.
DR OrthoDB; 193579at2; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000008330; 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..612
FT /note="Dihydroxy-acid dehydratase"
FT /id="PRO_1000089403"
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 612 AA; 65215 MW; 7261611BB17E8685 CRC64;
MPAYRSRTTT HGRNMAGARG LWRATGMKDS DFGKPIIAVV NSFTQFVPGH VHLKDLGQLV
AREIEAAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSRELI ADSVEYMVNA HCADAMVCIS
NCDKITPGML MASLRLNIPT VFVSGGPMEA GKVVLHGKTH ALDLVDAMVA AADEKISDED
VQTIERSACP TCGSCSGMFT ANSMNCLTEA LGLSLPGNGS TLATHADRKR LFVEAGHLIV
DLARRYYEQD DIKALPRTIA SKQAFENAMA LDIAMGGSTN TVLHILAAAH EGEIDFTMAD
IDALSRRVPC LSKVAPAKSD VHMEDVHRAG GIMSILGELD KGGLLNRNCP TVHAETLGDA
IDRWDITRTT SETVRNFYRA APGGIPTQVA FSQEARWDEL DTDRQNGVIR SVEHPFSRDG
GLAVLKGNLA VDGCIVKTAG VDESILKFSG PARVFESQDA SVKAILANEV KAGDVVVIRY
EGPKGGPGMQ EMLYPTSYLK SKGLGKACAL ITDGRFSGGT SGLSIGHASP EAANGGTIGL
VREGDMIDID IPNRTISLRV DEAELAARRA DQDAKGWHPA EVRKRNVTTA LKAYAAFATS
ADRGAVRDLN AR