ID ILVD_PELPD Reviewed; 553 AA.
AC A1AS43;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 01-MAY-2013, entry version 44.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; OrderedLocusNames=Ppro_2559;
OS Pelobacter propionicus (strain DSM 2379).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Pelobacteraceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Lovley D., Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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; CP000482; ABL00164.1; -; Genomic_DNA.
DR RefSeq; YP_902221.1; NC_008609.1.
DR ProteinModelPortal; A1AS43; -.
DR STRING; 338966.Ppro_2559; -.
DR EnsemblBacteria; ABL00164; ABL00164; Ppro_2559.
DR GeneID; 4572387; -.
DR KEGG; ppd:Ppro_2559; -.
DR PATRIC; 22898219; VBIPelPro64470_2716.
DR eggNOG; COG0129; -.
DR HOGENOM; HOG000173155; -.
DR KO; K01687; -.
DR OMA; VKKEGGI; -.
DR ProtClustDB; PRK00911; -.
DR BioCyc; PPRO338966:GHL0-2622-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 1 553 Dihydroxy-acid dehydratase.
FT /FTId=PRO_1000001026.
FT METAL 119 119 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 193 193 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 553 AA; 58509 MW; 35E0F10FF581CD2B CRC64;
MRSDTITQGF ERTPHRALLK GSGVPQSQMD KPFIGVATSF TDLIPGHVGM RDLERFIEKG
VHTGGGHAFF FGLPGVCDGI AMGHKGMHYS LPTRELIADM VESVAEAHRL DGLVLLTNCD
KITPGMLMAA ARLDIPCIVV TAGPMMSGRG QEGRKFSFVT DTFEAMARYK AGVISERELM
VCEENACPGI GSCQGLFTAN TMAILTETMG MSLPRCGTAL AVSALKRRIA FASGEKIVEL
VQNNITPRSI LTREAFENAI RVDLALGGSS NTVLHLLAIA NEAGVELPLE TFDILAKETP
QLASMNPAGE HFMEDLDVAG GVSGVMKQLG DKIKDTQTLF GLTTRQLAAS VENVDETVIR
PLTNPVKKEG GIAVLFGNIA PKGAVVKQSG VSDKMMKFEG TARCFDSEEL AMAALMEGEI
VAGNVVVIRY EGPKGGPGMR EMLAPTAALM GLGLGDSVAL ITDGRFSGGT RGPCIGHISP
EAAQGGPIGL IQDGDRISLD IPARRLELLV DEAVLQARAA TWVAPPPKIA KGWLARYAKV
VTSAHTGAVT TAE
//
