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 01-MAY-2013, entry version 29.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; 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;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Forester B., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Dunfield P.F.,
RA Dedysh S.N., Liesack W., Stott M.B., Smirnova A.V., Alam M., Chen Y.,
RA Murrell J.C., Richardson P.;
RT "Complete sequence of Methylocella silvestris BL2.";
RL Submitted (DEC-2008) 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; 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; QGRNMAG; -.
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 1 616 Dihydroxy-acid dehydratase.
FT /FTId=PRO_1000190671.
FT METAL 122 122 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 195 195 Iron-sulfur (4Fe-4S) (Potential).
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
//
