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
//