(data stored in ACNUC7421 zone)

SWISSPROT: ILVD_PSEAB

ID   ILVD_PSEAB              Reviewed;         612 AA.
AC   Q02U62;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=PA14_04630;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate
CC         + H2O; Xref=Rhea:RHEA:20936, ChEBI:CHEBI:11424,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377; EC=4.2.1.9;
CC         Evidence={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; CP000438; ABJ15317.1; -; Genomic_DNA.
DR   RefSeq; WP_003084436.1; NC_008463.1.
DR   SMR; Q02U62; -.
DR   EnsemblBacteria; ABJ15317; ABJ15317; PA14_04630.
DR   KEGG; pau:PA14_04630; -.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; IPGHVHL; -.
DR   BioCyc; PAER208963:G1G74-385-MONOMER; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000000653; 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-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.30.80; -; 1.
DR   HAMAP; MF_00012; IlvD; 1.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR004404; DihydroxyA_deHydtase.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; SSF143975; 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; Q02U62.
DR   SWISS-2DPAGE; Q02U62.
KW   4Fe-4S; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN         1    612       Dihydroxy-acid dehydratase.
FT                                /FTId=PRO_1000001034.
FT   METAL       122    122       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       193    193       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   612 AA;  65160 MW;  EE6C5F22697841F3 CRC64;
     MPDYRSKTST HGRNMAGARA LWRATGMKDE DFKKPIIAIA NSFTQFVPGH VHLKDLGQLV
     AREIEKAGGV AKEFNTIAVD DGIAMGHDGM LYSLPSREII ADSVEYMVNA HCADAIVCIS
     NCDKITPGML MAALRLNIPV VFVSGGPMEA GKTKLASHGL DLVDAMVVAA DDSCSDEKVA
     EYERSACPTC GSCSGMFTAN SMNCLTEALG LSLPGNGSTL ATHADREQLF LRAGRLAVEL
     CQRYYGEGDD SVLPRNIANF KAFENAMTLD IAMGGSTNTI LHLLAAAQEA EVPFDLRDID
     RLSRKVPQLC KVAPNIQKYH MEDVHRAGGI FSILGELARG GLLHTDVPTV HSPSMADAIA
     QWDITQTRDE AVHTFFKAGP AGIPTQTAFS QNTRWPSLDD DRAEGCIRSV EHAYSKEGGL
     AVLYGNIALD GCVVKTAGVD ESIHVFEGSA KIFESQDAAV KGILGDEVKA GDIVIIRYEG
     PKGGPGMQEM LYPTSYLKSK GLGKQCALLT DGRFSGGTSG LSIGHASPEA AAGGAIGLVQ
     DGDKVLIDIP NRSINLLVSD EELAARRAEQ DKKGWKPAAP RARRVSTALK AYALLATSAD
     KGAVRNKALL DG
//

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