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Database: UniProt
Entry: A8ZTQ7
LinkDB: A8ZTQ7
Original site: A8ZTQ7 
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   26-NOV-2014, entry version 49.
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=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. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [4Fe-4S] cluster. {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
CC       from pyruvate: step 3/4. {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; 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; CRWDSVD; -.
DR   OrthoDB; EOG6MSS24; -.
DR   BioCyc; DOLE96561:GHF3-2065-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:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-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; SSF52016; 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; Reference proteome.
FT   CHAIN         1    557       Dihydroxy-acid dehydratase.
FT                                /FTId=PRO_1000089380.
FT   METAL       119    119       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       194    194       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
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
//
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