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 01-MAY-2013, entry version 53.
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; PITIDIP; -.
DR ProtClustDB; PRK00911; -.
DR BioCyc; CCHL340177:GHBW-1875-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 1 559 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
//
