ID F0J5E3_ACIMA Unreviewed; 617 AA.
AC F0J5E3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 ECO:0000313|EMBL:BAJ80192.1};
GN OrderedLocusNames=ACMV_08450 {ECO:0000313|EMBL:BAJ80192.1};
GN ORFNames=Apmu_0178_01 {ECO:0000313|EMBL:GAN74480.1};
OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS 301).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ80192.1, ECO:0000313|Proteomes:UP000007100};
RN [1] {ECO:0000313|EMBL:BAJ80192.1, ECO:0000313|Proteomes:UP000007100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:BAJ80192.1}, and DSM 11245 / JCM 8867
RC / AIU301 {ECO:0000313|Proteomes:UP000007100};
RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA Hosoyama A., Yamada R., Fujita N.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAN74480.1, ECO:0000313|Proteomes:UP000032662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:GAN74480.1,
RC ECO:0000313|Proteomes:UP000032662};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (NOV-2012) 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; AP012035; BAJ80192.1; -; Genomic_DNA.
DR EMBL; BANA01000175; GAN74480.1; -; Genomic_DNA.
DR RefSeq; WP_007422795.1; NZ_BANA01000175.1.
DR AlphaFoldDB; F0J5E3; -.
DR SMR; F0J5E3; -.
DR KEGG; amv:ACMV_08450; -.
DR HOGENOM; CLU_014271_4_2_5; -.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000007100; Chromosome.
DR Proteomes; UP000032662; 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}.
FT ACT_SITE 516
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00012"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT MOD_RES 124
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
SQ SEQUENCE 617 AA; 65339 MW; 560B4A9F02D7007A CRC64;
MPQYRSRTST HGRNMAGARA LWRATGMGDA DFGKPIIAIA NSFTQFVPGH VHLKDLGQLV
AREIEAAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI ADAVEYMVNA HCADALVCIS
NCDKITPGML MAAMRLNIPT IFVSGGPMEA GKYIADGETR AADLITAMVV AADPTKTDEQ
AAVMERSACP TCGSCSGMFT ANSMNCLTEA LGLALPGNGS LLATHADRKR LFVEAGWQIV
DLARRYYEQD DEGVLPRRIG GFKAFENAMS LDIAMGGSTN TVLHLLAAAR EAELDFTMAD
IDRLSRRVPN LCKVSPSVSN VHMEDVHRAG GIMGILGALD RAGLIHRDCA TVHEKTIGEA
IDRWDVMRGG ETAKTLYSAA PGGVRTTEAF SQSRRYESLD LDREKGVIRD AEHAFSKDGG
LAVLYGNIAL DGAIVKTAGV DASILVFEGP ARIFESQEDA VAGILGDRVK AGDVVLIRYE
GPKGGPGMQE MLYPTSYLKS KGLGKSCALI TDGRFSGGTA GLSIGHISPE AAQGGAIGLV
EEGDIIAIDI PNRKLDVKLD EATLEARRAA MEAKGKAAWK PAARERVVSA ALQAYAALTT
SAANGAVRDV TQVQRGR
//
