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Database: UniProt
Entry: A7ZTX3
LinkDB: A7ZTX3
Original site: A7ZTX3 
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   14-MAY-2014, entry version 48.
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; CRWDSVD; -.
DR   OrthoDB; EOG6MSS24; -.
DR   BioCyc; ECOL331111:GH7P-4260-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.
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
//
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