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Database: UniProt
Entry: B8EQC8
LinkDB: B8EQC8
Original site: B8EQC8 
ID   ILVD_METSB              Reviewed;         616 AA.
AC   B8EQC8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   26-NOV-2014, entry version 36.
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=Msil_3234;
OS   Methylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL2 / DSM 15510 / NCIMB 13906;
RX   PubMed=20472789; DOI=10.1128/JB.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK52141.1; -; Genomic_DNA.
DR   RefSeq; YP_002363503.1; NC_011666.1.
DR   STRING; 395965.Msil_3234; -.
DR   EnsemblBacteria; ACK52141; ACK52141; Msil_3234.
DR   GeneID; 7090649; -.
DR   KEGG; msl:Msil_3234; -.
DR   PATRIC; 22602238; VBIMetSil55537_3469.
DR   eggNOG; COG0129; -.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; CRWDSVD; -.
DR   OrthoDB; EOG6MSS24; -.
DR   BioCyc; MSIL395965:GCND-3286-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    616       Dihydroxy-acid dehydratase.
FT                                /FTId=PRO_1000190671.
FT   METAL       122    122       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       195    195       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   616 AA;  65213 MW;  DA13E14786F78EFD CRC64;
     MPPYRSRTTT HGRNMAGARG LWRATGMKDG DFGKPIIAVA NSFTQFVPGH VHLKDLGQLV
     AREIEAAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSREII ADSVEYMVNA HCADAIVCIS
     NCDKITPGML MASLRLNIPV VFVSGGPMEA GKVLLGGKTK ALDLVDAMVA AADDKVSEAD
     VAAIERSACP TCGSCSGMFT ANSMNCLTEA LGLALPGNGS MLATHGDRKR LFVEAGHLIV
     DLARRYYEQD DSSVLPRSIA SFAAFENAMT LDISMGGSTN TVLHLLAAAH EGEIDFTMAD
     IDRLSRRVPV LCKVAPAVAD VHVEDVHRAG GVMAILGELE RAGLIHGDLP VVHAPSLKEA
     LERWDLRRTS SESVTEFFRA APGGVPTQVA FSQNARWKET DVDRAGGVIR DVEHAFSKDG
     GLAVLYGNLA EDGAIVKTAG VDASILVFSG PARVFESQDA AVEAILANQI KPGDVLVIRY
     EGPRGGPGMQ EMLYPTSYLK SKGLGKACAL ITDGRFSGGT SGLSIGHVSP EAAEGGLIGL
     VEEGDSIQID IPNRRLHLDI SDEALAHRRT AMAEKGKGAW KPAHRTRKVS TALRAYAAMA
     TSAARGAVRD VDQLFH
//
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