ID ILVD_CALBD Reviewed; 552 AA.
AC B9MPM8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 34.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; OrderedLocusNames=Athe_0665;
OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS (Anaerocellum thermophilum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis;
OC Caldicellulosiruptor.
OX NCBI_TaxID=521460;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Kataeva I., Adams M.W.W.;
RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM
RT 6725.";
RL Submitted (JAN-2009) 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; CP001393; ACM59789.1; -; Genomic_DNA.
DR RefSeq; YP_002572562.1; NC_012034.1.
DR STRING; 521460.Athe_0665; -.
DR EnsemblBacteria; ACM59789; ACM59789; Athe_0665.
DR GeneID; 7407089; -.
DR KEGG; ate:Athe_0665; -.
DR PATRIC; 20898362; VBIAnaThe135187_0704.
DR eggNOG; COG0129; -.
DR HOGENOM; HOG000173156; -.
DR KO; K01687; -.
DR OMA; GATPMEF; -.
DR ProtClustDB; PRK00911; -.
DR BioCyc; CBES521460:GH8H-688-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 1 552 Dihydroxy-acid dehydratase.
FT /FTId=PRO_1000116496.
FT METAL 119 119 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 191 191 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 552 AA; 58914 MW; C2C864A26B53AF4C CRC64;
MRSDTVKKGF EKAPQRSLFK AMGYTDEEIR RPLIAVVNSW NEVVPGHIHL DRIAEAVKAG
IRLAGATPME FNVIGVCDGI AMGHIGMKYS LITRELIADS IEAMVMAHQF DGMVLIPNCD
KIVPGMLIAA ARVNIPAILI SGGPMLAGKI GDKVCDLNSV FEGVGAYSAG KISEEDLYAL
EENACPGCGS CSGMFTANTM NCLSEVLGLA LPGNGTIPAV MAARIRLAKM AGMKIVELVE
KDIKPSDILT VEAFENALAV DMALGGSTNT ILHLPAIANE VGIKLNLDII NAISDRTPNL
CKLSPAGQHH IEDLYFAGGV QAVMNELSKK GLLHLNLMTV TGKTVGENIK DANVKNYNVI
RPIDNPYSET GGLVIVRGNL APDGAVVKKS AVPPKLMKHR GPARVFESGE EVFEAILKGK
IQKGDVIVIR YEGPKGGPGM REMLSPTSAL AGVGLIEDVA LITDGRFSGA TRGACFGHVS
PEAAERGPIA AVQDGDMISI DIENKTLTLE VPEEEIKRRL EILPPFEPKV KKGYLYRYSK
LVRSASTGAI LE
//
