ID ILVD_ECO24 Reviewed; 616 AA.
AC A7ZTX3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 01-MAY-2013, entry version 43.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; OrderedLocusNames=EcE24377A_4282;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/JB.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic
RT analysis of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV17245.1; -; Genomic_DNA.
DR RefSeq; YP_001465252.1; NC_009801.1.
DR ProteinModelPortal; A7ZTX3; -.
DR SMR; A7ZTX3; 65-611.
DR STRING; 331111.EcE24377A_4282; -.
DR EnsemblBacteria; ABV17245; ABV17245; EcE24377A_4282.
DR GeneID; 5589972; -.
DR KEGG; ecw:EcE24377A_4282; -.
DR PATRIC; 18297838; VBIEscCol31211_4516.
DR eggNOG; COG0129; -.
DR HOGENOM; HOG000173155; -.
DR KO; K01687; -.
DR OMA; QGRNMAG; -.
DR ProtClustDB; PRK12448; -.
DR BioCyc; ECOL331111:GH7P-4289-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 1 616 Dihydroxy-acid dehydratase.
FT /FTId=PRO_1000057096.
FT METAL 122 122 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 195 195 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 616 AA; 65532 MW; 352FC303DCFF2109 CRC64;
MPKYRSATTT HGRNMAGARA LWRATGMTDA DFGKPIIAVV NSFTQFVPGH VHLRDLGKLV
AEQIEAAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI ADSVEYMVNA HCADAMVCIS
NCDKITPGML MASLRLNIPV IFVSGGPMEA GKTKLSDQII KLDLVDAMIQ GADPKVSDSQ
SDQVERSACP TCGSCSGMFT ANSMNCLTEA LGLSQPGNGS LLATHADRKQ LFLNAGKRIV
ELTKRYYEQN DESALPRNIA SKAAFENAMT LDIAMGGSTN TVLHLLAAAQ EAEIDFTMSD
IDKLSRKVPQ LCKVAPSTQK YHMEDVHRAG GVIGILGELD RAGLLNRDVK NVLGLTLPQT
LEQYDVMLTQ DDAVKNMFRA GPAGIRTTQA FSQDCRWDSL DDDRANGCIR SLEHAYSKDG
GLAVLYGNFA ENGCIVKTAG VDDSILKFTG PAKVYESQDD AVEAILGGKV VAGDVVVIRY
EGPKGGPGMQ EMLYPTSFLK SMGLGKACAL ITDGRFSGGT SGLSIGHVSP EAASGGSIGL
IEDGDLIAID IPNRGIQLQV SDAELAARRE AQEARGDKAW TPKNRERQVS FALRAYASLA
TSADKGAVRD KSKLGG
//
