(data stored in ACNUC7421 zone)

SWISSPROT: ILVD_EDWI9

ID   ILVD_EDWI9              Reviewed;         616 AA.
AC   C5BBA5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
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=NT01EI_0080;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001600; ACR67340.1; -; Genomic_DNA.
DR   RefSeq; WP_015869561.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0080; -.
DR   EnsemblBacteria; ACR67340; ACR67340; NT01EI_0080.
DR   GeneID; 7959799; -.
DR   KEGG; eic:NT01EI_0080; -.
DR   PATRIC; fig|634503.3.peg.73; -.
DR   eggNOG; ENOG4105C01; Bacteria.
DR   eggNOG; COG0129; LUCA.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; IPGHVHL; -.
DR   OrthoDB; POG091H010A; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000001485; Chromosome.
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-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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   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;
DR   PRODOM; C5BBA5.
DR   SWISS-2DPAGE; C5BBA5.
KW   4Fe-4S; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Lyase; Metal-binding; Reference proteome.
FT   CHAIN         1    616       Dihydroxy-acid dehydratase.
FT                                /FTId=PRO_1000201776.
FT   METAL       122    122       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       195    195       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   616 AA;  65804 MW;  7D66D37B1E976006 CRC64;
     MPKYRSATTT HGRNMAGARA LWRATGMTDA DFGKPIIAVV NSFTQFVPGH VHLRDLGRLV
     AAQIEATGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI ADSVEYMVNA HCADAMVCIS
     NCDKITPGMM MAALRLNIPV IFVSGGPMEA GKTKLSDRLI KLDLVDAMIQ GANPQVSDAQ
     SEQIERAACP TCGSCSGMFT ANSMNCLTEA LGLALPGNGS LLATHADRRA LFEEAGQRIV
     ALTRRYYEQD DVSVLPRSIA CKAAFENAMT LDIAMGGSTN TVLHLLAAAQ EGEIDFTLAD
     IDRLSRQVPH LCKVAPSTPD YHMEDVHRAG GVMGILGELD RAGLLNRGVA NVLGLGLSET
     LARYDIMRSD DDALQRLYRA GPAGLRTVEP FAQSCRWDAL DRDRQQGCIR AREHAYSQDG
     GLAVLSGNLA QDGCIVKTAG VDPDSLVFRG PARVFESQEE AVEAILGGRI HPGDVLVIRY
     EGPKGGPGMQ EMLYPTAYLK SMGLGKQCAL ITDGRFSGGT SGLSIGHVSP EAASGGAIAL
     VRDGDPIEID IPVRHIRLAI AESELALRRQ QELARGTQAW TPRDRRRKVS LALRAYASLA
     TSADRGAVRD RAKLGG
//

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