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Database: UniProt
Entry: C5CU92_VARPS
LinkDB: C5CU92_VARPS
Original site: C5CU92_VARPS 
ID   C5CU92_VARPS            Unreviewed;       578 AA.
AC   C5CU92;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ACS20305.1};
DE            EC=4.2.1.9 {ECO:0000313|EMBL:ACS20305.1};
GN   OrderedLocusNames=Vapar_3689 {ECO:0000313|EMBL:ACS20305.1};
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS20305.1};
RN   [1] {ECO:0000313|EMBL:ACS20305.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S110 {ECO:0000313|EMBL:ACS20305.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA   Leadbetter J.R., Spain J.C., Han J.I.;
RT   "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
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DR   EMBL; CP001635; ACS20305.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5CU92; -.
DR   STRING; 543728.Vapar_3689; -.
DR   KEGG; vap:Vapar_3689; -.
DR   eggNOG; COG0129; Bacteria.
DR   HOGENOM; CLU_014271_3_1_4; -.
DR   OrthoDB; 9807077at2; -.
DR   GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACS20305.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   578 AA;  62971 MW;  C43193DDF5360FBB CRC64;
     MSTSPKKKPE DLRSQQWFGR HDRDGFIYRS WVKGKGVPHD QFDGRPVIGI CNTFSELTPC
     NSHFRTLAEQ VKIGVYEAGG FPLEFPVMSL GETLLRPTAM LYRNLASMDV EESIRGNPLD
     GVVLLMGCDK TTPALMMGAA SVDLPTIGVS GGPMLSGKWR GQELGSGTGV WQMSEQVRAG
     TLKLQDFFEA ESCMHRSHGH CMTMGTASTM ASMVESLGIG LPGNAAYPAV DGRRNVLARM
     AGRRIVDMVH EDLHMSKILT RQAIENAIKV NAAIGGSTNL VIHLLAIAGR IGVDLSLDDF
     DRLASDLPCL VDLQPSGRFL MEDFCYAGGL PVVIKEIAQY LHKDVITANG QTLWDNVKDA
     ENYNPQVIRP LAEPFKDKAG ICVLRGNLAP NGAIIKPSAA TPELLVHKGR AVVFESADDL
     HKRIDDENLD IDEHCVMVLK NCGPRGYPGM AESGNMPLPP KVLRKGITDM VRISDARMSG
     TAYGTVVLHT APEAAAGGPL ALVQDGDIVE LDVPNRKLHL HVSDEELARR LEKWVAPKAP
     LDSGYWKLYV DTVLQADQGA DLAFLRGRRG AFVPRDNH
//
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