(data stored in ACNUC7421 zone)

SWISSPROT: Q13RF7_PARXL

ID   Q13RF7_PARXL            Unreviewed;       620 AA.
AC   Q13RF7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00636246};
DE            Short=DAD {ECO:0000256|HAMAP-Rule:MF_00012};
DE            EC=4.2.1.9 {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00636246};
GN   Name=ilvD {ECO:0000256|HAMAP-Rule:MF_00012};
GN   ORFNames=Bxe_B2661 {ECO:0000313|EMBL:ABE33332.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33332.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33332.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33332.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-
CC       oxobutanoate + H(2)O. {ECO:0000256|HAMAP-Rule:MF_00012,
CC       ECO:0000256|SAAS:SAAS00636149}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00012, ECO:0000256|SAAS:SAAS00636203}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 3/4. {ECO:0000256|HAMAP-Rule:MF_00012,
CC       ECO:0000256|SAAS:SAAS00636239}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000256|HAMAP-
CC       Rule:MF_00012, ECO:0000256|SAAS:SAAS00543775}.
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DR   EMBL; CP000271; ABE33332.1; -; Genomic_DNA.
DR   RefSeq; WP_011490701.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2661; -.
DR   EnsemblBacteria; ABE33332; ABE33332; Bxe_B2661.
DR   GeneID; 4006623; -.
DR   KEGG; bxb:DR64_4995; -.
DR   KEGG; bxe:Bxe_B2661; -.
DR   PATRIC; fig|266265.5.peg.5040; -.
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; UP000001817; Chromosome 2.
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-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-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   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; Q13RF7.
DR   SWISS-2DPAGE; Q13RF7.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00636254};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00636179};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_00012, ECO:0000256|SAAS:SAAS00636187};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00636142};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00636271};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00427188,
KW   ECO:0000313|EMBL:ABE33332.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00636228};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   METAL       122    122       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       198    198       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   620 AA;  65682 MW;  3E4C41B793289AAE CRC64;
     MPEYRSRTST HGRNMAGARA LWRATGMKDG DFGKPIIAVV NSFTQFVPGH VHLRDLGALV
     AKEIEAAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI ADSVEYMVNA HCADAMVCIS
     NCDKITPGML MAAMRLNIPV VFVSGGPMEA GKVKSPKDGQ VIAKIDLIDA MIKAADSKVS
     DAEVAEIERS ACPTCGSCSG MFTANSMNCL TEAIGLALPG NGTIVATHAW RKDLFEQAGR
     LVVDLCRRYY QEEDTSVLPR SIASKQAFEN AMALDVAMGG STNTVLHLLA AAQEAGVDFT
     MSDIDRISRK VPCLCKAAPA TDKYHIEDVH RAGGILGILG ELARADLLDL SCGNVHSGTL
     GDAIARWDIA GGAGEEAQKF FRAAPGGIPT TVAFSQEATF PSLDTDRKTG CIRSKQDAYS
     KDGGLAVLYG NLAEKGCIVK TAGVDESQWV FSGRARVFES QDDAVEAILG DKVVAGDVVV
     IRYEGPKGGP GMQEMLYPTS YLKSKGLGKT CALFTDGRFS GGSSGLVIGH ASPEAAEGGT
     IGLVEEGDVI EIDIPKRKMH LVVSDGELAR RREAMEARGD KAWMPAARER VVSQALQAYA
     ALATSADRGA VRDISQLKRK
//

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