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Database: UniProt
Entry: Q3APB9
LinkDB: Q3APB9
Original site: Q3APB9 
ID   ILVD_CHLCH              Reviewed;         559 AA.
AC   Q3APB9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   19-FEB-2014, entry version 57.
DE   RecName: Full=Dihydroxy-acid dehydratase;
DE            Short=DAD;
DE            EC=4.2.1.9;
GN   Name=ilvD; OrderedLocusNames=Cag_1906;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000108; ABB29156.1; -; Genomic_DNA.
DR   RefSeq; YP_380199.1; NC_007514.1.
DR   ProteinModelPortal; Q3APB9; -.
DR   STRING; 340177.Cag_1906; -.
DR   EnsemblBacteria; ABB29156; ABB29156; Cag_1906.
DR   GeneID; 3747651; -.
DR   KEGG; cch:Cag_1906; -.
DR   PATRIC; 21371584; VBIChlChl46571_1985.
DR   eggNOG; COG0129; -.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; IPGHVHL; -.
DR   OrthoDB; EOG6MSS24; -.
DR   ProtClustDB; PRK00911; -.
DR   BioCyc; CCHL340177:GHBW-1921-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    559       Dihydroxy-acid dehydratase.
FT                                /FTId=PRO_0000225382.
FT   METAL       121    121       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       194    194       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   559 AA;  58691 MW;  0683F9E2FAB7B5ED CRC64;
     MRSDTIKSGF EKAPHRSLLK ATGAIRSSSD YRKPFIGICN SYNELIPGHT HLQELGRIAK
     EAVREAGGVP FEFNTIGVCD GIAMGHIGMR YSLASRELIA DSVETVAEAH RLDGLVCIPN
     CDKITPGMMM AALRINIPVI FVSGGPMKAG HTPEGKTVDL ISVFEAVGQC SNGSITEGEL
     QNIEEHACPG CGSCSGMFTA NSMNCLSEAL GFALPGNGTI VAEDPRRLEL VKAASRRIVD
     LVENNVRPRD ILTRQALLNA FALDFAMGGS TNTILHTLAI ANEAGLSFDF SELNALSAKT
     PYICQVSPAT MAVHIEDVDR AGGISAILKE LSSIDGLLDL SAITVTGKTL GENIANAEVL
     DRSVIRSISD PYSATGGLAV LYGNLAPQGA VVKTGAVSPQ MMQHSGPAKV YNAQDDAIKG
     IMEGDVKAGD VVVIRYEGPK GGPGMPEMLS PTSAIMGRGL GDSVALITDG RFSGGSRGAC
     IGHVSPEAAE RGPIAALQNG DIITIDIPAR TMSVALSEST IKERLAQLPP FEPKIKRGYL
     ARYAQLVTSA NTGAILGHL
//
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