ID E8U7W5_DEIML Unreviewed; 566 AA.
AC E8U7W5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Deima_1505 {ECO:0000313|EMBL:ADV67154.1};
OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 /
OS LB-34).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV67154.1, ECO:0000313|Proteomes:UP000008635};
RN [1] {ECO:0000313|EMBL:ADV67154.1, ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RX PubMed=21677853; DOI=10.4056/sigs.1633949;
RA Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Deinococcus maricopensis type strain (LB-
RT 34).";
RL Stand. Genomic Sci. 4:163-172(2011).
RN [2] {ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N.,
RA Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Deinococcus maricopensis DSM 21211.";
RL Submitted (JAN-2011) 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; CP002454; ADV67154.1; -; Genomic_DNA.
DR RefSeq; WP_013556659.1; NC_014958.1.
DR AlphaFoldDB; E8U7W5; -.
DR STRING; 709986.Deima_1505; -.
DR KEGG; dmr:Deima_1505; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_4_2_0; -.
DR OrthoDB; 9807077at2; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000008635; 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 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:UP000008635}.
FT ACT_SITE 482
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT BINDING 133
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 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT MOD_RES 133
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
SQ SEQUENCE 566 AA; 60576 MW; 602D3FA8CD549891 CRC64;
MTIKDKPQLK QRSSTIKEGF ERAPHRSLLR ATGVIERESD FGKPFIAICN SYIDIIPGHV
HLQEFGRIVK EAVRAAGGVP FEFNTIGVDD GIAMGHTGMK YSLPSRELIA DAVETVVEAH
QFDAMICIPN CDKIVPGMLM GAMRCDIPTI FISGGPMMRG LSKTGERLDL TKMFEAVGAY
QAGKLDMETL TDMEQNACPT CGSCSGMFTA NSMNCLCEAL GMALPGNGTI PATDPRRHEL
ARAAAKQVMV LLERGITPRQ IVTAEAIDNA FALDMAMGGS TNTVLHTLAI AHEIGVEYPL
SRLNEVSDRV PNLCKLAPMS NFHMQDLDEV GGVSVIIKAL FEHEGIMHRG CMTATGQVLE
DNVADAPDAD GQVVRTWDNA YSRTGGLRLL FGNLAPEGGV IKYAGVVPSM RQFEGEAIVF
DSMEAANEGI LGGQVRAGHV VVIRYEGPQG GPGMQEMLSP TANIAGMGLG ESVLLLTDGR
FSGATRGGSI GHISPEASAG GPIAFVRNGD RIRVDMDAGQ LELLVSAEEL DARREGWVPV
VKPIPGKWLK RYARLVTSGS RGAVLV
//
