ID ILVD_CAMHC Reviewed; 553 AA.
AC A7I439;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 01-MAY-2013, entry version 41.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; OrderedLocusNames=CHAB381_1769;
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
RL Submitted (JUL-2007) 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; CP000776; ABS51486.1; -; Genomic_DNA.
DR RefSeq; YP_001407280.1; NC_009714.1.
DR STRING; 360107.CHAB381_1769; -.
DR EnsemblBacteria; ABS51486; ABS51486; CHAB381_1769.
DR GeneID; 5409052; -.
DR KEGG; cha:CHAB381_1769; -.
DR PATRIC; 20041638; VBICamHom81367_1685.
DR eggNOG; COG0129; -.
DR HOGENOM; HOG000173155; -.
DR KO; K01687; -.
DR OMA; QGRNMAG; -.
DR ProtClustDB; PRK00911; -.
DR BioCyc; CHOM360107:GHCX-1774-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 1 553 Dihydroxy-acid dehydratase.
FT /FTId=PRO_1000000971.
FT METAL 119 119 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 192 192 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 553 AA; 59425 MW; 26D2881C75D4B2DB CRC64;
MRSDVIKKGY IRAPHRSLLR ATGLKDDDFK KPFIGVCNSF AEIIPGHFFL NKFAKIIKDE
IRKNGCVPFE FNCIGVDDGI AMGHDGMLYS LPSREIIANS VETMMNAHKL DALICIPNCD
KIVPGMIMGA LRVNVPTIFI SGGPMAAGRG KNGEALDLNS TFEAVGAYEV KKINKKELHD
IECAACPGAG SCSGMFTANS MNTLCEAMGI ALKGNGTILA MTKNRKKLAK KAARRICEIA
LDDKFKIRNI INKKAVENAM VVDMAMGGSS NTILHMLAIS REAGCALDIK ELNEISKKTP
HIAKIAPSKP EIHMQDVHNA GGINAIMNEV KDLLHLDNLT VTGETLGERI KGAKIKDEDV
IHKVENAYSK VGGLAILFGN LAEQGCVIKA AGIIGSRKFS GKAICFNSQD EAIEGISGGK
VKKGDVVVIR YEGPKGGPGM QEMLSPTSLI VGRGLGADVA LITDGRFSGA TRGLCIGHVS
PEAAEGGMIG LLKDGDIIDI DVDNFSINVR LSEDEIAERK KEFKYGGKKV QSRWLRQYQK
LVTNASNGAI LEA
//
