ID ILVD_DESOH Reviewed; 557 AA.
AC A8ZTQ7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 01-MAY-2013, entry version 42.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; OrderedLocusNames=Dole_2036;
OS Desulfococcus oleovorans (strain DSM 6200 / Hxd3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfococcus.
OX NCBI_TaxID=96561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / Hxd3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Wawrik B., Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-
CC oxobutanoate + H(2)O.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 3/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC from pyruvate: step 3/4.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
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DR EMBL; CP000859; ABW67840.1; -; Genomic_DNA.
DR RefSeq; YP_001529917.1; NC_009943.1.
DR STRING; 96561.Dole_2036; -.
DR EnsemblBacteria; ABW67840; ABW67840; Dole_2036.
DR GeneID; 5694879; -.
DR KEGG; dol:Dole_2036; -.
DR PATRIC; 21694199; VBIDesOle35880_2101.
DR eggNOG; COG0129; -.
DR HOGENOM; HOG000173156; -.
DR KO; K01687; -.
DR OMA; QGRNMAG; -.
DR ProtClustDB; PRK00911; -.
DR BioCyc; DOLE96561:GHF3-2087-MONOMER; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:HAMAP.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00012; IlvD; 1; -.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR004404; DihydroxyA_deHydtase.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR PANTHER; PTHR21000; PTHR21000; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 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 4Fe-4S; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW Iron-sulfur; Lyase; Metal-binding.
FT CHAIN 1 557 Dihydroxy-acid dehydratase.
FT /FTId=PRO_1000089380.
FT METAL 119 119 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 194 194 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 557 AA; 58232 MW; C7C41EA19D9F758B CRC64;
MKSDSMKEGL ARAPHRSLLK SIGYTDEEIG RPIIGIVNSA NEIVPGHADL NKIARAVKDG
VYMAGGTPVE FSTIGVCDGI AMNHIGMKYS LGSRELIADS VEIMATAHAF DALVMIPNCD
KIVPGMLMAA ARLNLPTIFI SGGPMLAGRY PGKPEKKVDL ITVFEAVGAV KSGRMAPEEL
AIIEDAACPT CGSCSGMFTA NSMNCLTEAI GMGLPGNGTV PAVMSERVRM AKQAGMRILD
LLKNGVTPDK IMTAKAFRNA LAVDMALGCS TNTVLHLPAI AHEAGVSISL DLINEISGIA
PHLCSLSPAG PNHIEDLNMA GGIQAVLKEL ARKSGLIDPD CLTVTGRTVG ENIASARDAD
GQVIRTLETP HHAQGGLAVL FGNLAPDGCV VKQSAVVDKM LVHEGPARVF DSEEDATTAI
MDGRIKKGDV LVIRYEGPKG GPGMREMLTP TSALAGMGLD STVALITDGR FSGGSRGAAI
GHVSPEAMEG GPIAVVKEGD TITIDIPKKK IGLKLDAGEI QNRLSGWNRP APKITRGYMA
RYADQVSSAN TGAIFKK
//
