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Database: UniProt
Entry: Q9RQ52
LinkDB: Q9RQ52
Original site: Q9RQ52 
ID   ILVD_BUCSC              Reviewed;         613 AA.
AC   Q9RQ52;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   01-OCT-2014, entry version 54.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012};
DE            Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012};
DE            EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012};
GN   Name=ilvD {ECO:0000255|HAMAP-Rule:MF_00012};
OS   Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10555290; DOI=10.1093/oxfordjournals.molbev.a026071;
RA   Clark M.A., Moran N.A., Baumann P.;
RT   "Sequence evolution in bacterial endosymbionts having extreme base
RT   compositions.";
RL   Mol. Biol. Evol. 16:1586-1598(1999).
CC   -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-
CC       oxobutanoate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. {ECO:0000255|HAMAP-
CC       Rule:MF_00012}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-
CC       Rule:MF_00012}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC       Rule:MF_00012}.
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DR   EMBL; AF130813; AAF13802.1; -; Genomic_DNA.
DR   PRIDE; Q9RQ52; -.
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; Iron; Iron-sulfur; Lyase;
KW   Metal-binding.
FT   CHAIN         1    613       Dihydroxy-acid dehydratase.
FT                                /FTId=PRO_0000103451.
FT   METAL       122    122       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       195    195       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   613 AA;  66960 MW;  A0359A0A2CB96F8F CRC64;
     MPKYRSSTTT QGRNMAGARA LWKATGMTDS DFNKPIIAVV NSFTEFVPGH IHLKELGTLV
     SSIIKLEGGV AKEFNTIAID DGIAMGHSGM LYSLPSRELI ADSIEYMINA HCADAMICIS
     NCDKITPGML MAALRLNIPC VFVSGGPMES GRIVVDGKEI KINLVDAIVY GANPNYSDAL
     ASRIENCACP TCGSCSGLFT ANSMNCLTEA LGLSLPGNGT LLATHIDRKK LFIDSGKLIV
     KITKEYYEDN NTSFLPRSIA SRESFLNAMS LDISTGGSTN TILHLLAMAQ EGQVDFKMSD
     IDLLSRKIPN LCKIAPNSDV YHMEDFHRAG GVIGLLAELN RVSLLNNNVK NILGLSLDVV
     LNKYDILKTK NQDVIEMFHA GPLGNKTSIP FTQSYRWKSL DKDRKKGCIR SYENAFSYDG
     GLAILYGNIA KNGCVVKTAG VKKGNLIFEG FAIVFESQEE ALKAILENKV KKGHVVVIRY
     EGPKGGPGMQ EMLYPTTYLK SMNLDEHCAL ITDGRFSGGT SGLSIGHISP EAANKGNIAL
     IRNNDVININ IPNRTINLDI TNDEFLNRMH NEIQRGKSSY TPQFRKRFVS SALKMYALFA
     TSADKGAVRK IQY
//
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