ID ILVD_BRUAB Reviewed; 611 AA.
AC Q57FS2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; OrderedLocusNames=BruAb1_0096;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Brucellaceae; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L.,
RA Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison
RT to the highly similar genomes of Brucella melitensis and Brucella
RT suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX73512.1; -; Genomic_DNA.
DR RefSeq; YP_220873.1; NC_006932.1.
DR STRING; 262698.BruAb1_0096; -.
DR PRIDE; Q57FS2; -.
DR EnsemblBacteria; AAX73512; AAX73512; BruAb1_0096.
DR GeneID; 3339002; -.
DR KEGG; bmb:BruAb1_0096; -.
DR PATRIC; 17821723; VBIBruAbo15061_0105.
DR eggNOG; COG0129; -.
DR HOGENOM; HOG000173155; -.
DR KO; K01687; -.
DR OMA; QGRNMAG; -.
DR ProtClustDB; PRK12448; -.
DR BioCyc; BABO262698:GJC2-97-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 1 611 Dihydroxy-acid dehydratase.
FT /FTId=PRO_0000225375.
FT METAL 122 122 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 195 195 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 611 AA; 65310 MW; EB112A030C2D7831 CRC64;
MPPYRSRTTT HGRNMAGARG LWRATGMKDE DFGKPIIAVV NSFTQFVPGH VHLKDLGQLV
AREIESAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSRELI ADSVEYMVNA HCADAMVCIS
NCDKITPGML MAALRLNIPV VFVSGGPMEA GKVVWEDSVK KLDLVDAMVA AADDHYTDEQ
VKAIERSACP TCGSCSGMFT ANSMNCLTEA LGLSLPGNGS TLATHADRKR LFVEAGHLIV
DLARRYYEQD DESVLPRSIA TFSAFENAMT LDIAMGGSTN TVLHLLAAAQ EAEIDFTMAD
IDRLSRRVPV LCKVAPAVSS VHMEDVHHAG GIMGILGQLD NAGLLTTSIP TVHSETLAKA
LDHWDVTRTN SEMVHKFYSA APGGVPTQVA FSQERRFDKV DTDREKGVIR SKEHAFSQDG
GLAVLYGNLA EDGCIVKTAG VDDSILKFSG PARIFESQDS AVLGILNGKI KPGDIVLIRY
EGPRGGPGMQ EMLYPTSYLK SKGLGKACAL ITDGRFSGGS SGLSIGHVSP EAAEGGTIGL
VREGDIIDID IPNRKIHLAV DDATLAERRA EQDAAGWKPA EERKRKISTA LKAYAAMATS
AARGAVRKLP D
//
