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Database: UniProt
Entry: Q04RA5
LinkDB: Q04RA5
Original site: Q04RA5 
ID   ILVD_LEPBJ              Reviewed;         560 AA.
AC   Q04RA5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   26-NOV-2014, entry version 52.
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};
GN   OrderedLocusNames=LBJ_2063;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A.,
RA   Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P.,
RA   Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
CC   -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-
CC       oxobutanoate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-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; CP000350; ABJ76565.1; -; Genomic_DNA.
DR   RefSeq; YP_801323.1; NC_008510.1.
DR   ProteinModelPortal; Q04RA5; -.
DR   STRING; 355277.LBJ_2063; -.
DR   EnsemblBacteria; ABJ76565; ABJ76565; LBJ_2063.
DR   GeneID; 4410841; -.
DR   KEGG; lbj:LBJ_2063; -.
DR   PATRIC; 22359860; VBILepBor13265_2634.
DR   eggNOG; COG0129; -.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; PENQDVI; -.
DR   OrthoDB; EOG6MSS24; -.
DR   BioCyc; LBOR355277:GHYM-2038-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    560       Dihydroxy-acid dehydratase.
FT                                /FTId=PRO_1000000998.
FT   METAL       125    125       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       197    197       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   560 AA;  59445 MW;  A00F61DB3743235D CRC64;
     MSDILKKRSS MTTDGDNRAP NRAMLRAVGF TDEDFHKPMI GIASTWSEVT PCNIHINKLA
     EKVKEGVRTA GGVPQIYGTI TVSDGITMGH EGMHFSLPSR EVIADSIEIV SNAMRHDGVI
     AIGGCDKNMP GCLMALCRID APSIFVYGGT ILPGHCDGQD VDIVSIFEAV GKFNAGKISR
     EEFIRIEQNA CPGAGSCGGM YTANTMSSAI EALGMSLPGS ASMPAVSSRK SEDCYEAGKA
     LINLIQKGVT PKRILTKKAF ENAITVVLVL GGSTNAVLHL IAIAKEIGVD LTLEDFDRIS
     KKTPHLADLK PGGRYAMTDL DKVGGVHGVM KYLLKEGMLH GDCLTVTGKT IAENLMDMPD
     LVPNQTIVRK KSEALHPSGP LVILKGNLAP EGAVAKISGL KKISITGPAK VFESEDDCFN
     AIMTDQIKPG DVIIIRYEGP KGGPGMREML AVTSALVGKG LGEDVGLMTD GRFSGGTHGL
     VVGHISPEAF DGGPIAIVQN GDAVTIDSGK NLLQVEISQE EIQKRLKNWK PIEPRYKSGV
     LAKYAKLVQS ATNGAITNLL
//
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