ID D5VNB1_CAUST Unreviewed; 591 AA.
AC D5VNB1;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ADG11984.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:ADG11984.1};
GN OrderedLocusNames=Cseg_3556 {ECO:0000313|EMBL:ADG11984.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG11984.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP002008; ADG11984.1; -; Genomic_DNA.
DR RefSeq; WP_013080630.1; NC_014100.1.
DR AlphaFoldDB; D5VNB1; -.
DR STRING; 509190.Cseg_3556; -.
DR KEGG; cse:Cseg_3556; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_5; -.
DR Proteomes; UP000002629; Chromosome.
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:ADG11984.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 591 AA; 64215 MW; 8EA5ADEB1C598162 CRC64;
MSERTPRRFR SRDWFDNPDH IDMTALYLER FMNYGITPEE LRSGKPIIGI AQTGSDISPC
NRIHLDLVTR IRDGIRDAGG IPMEFPVHPI FENCRRPTAA LDRNLSYLGL VETLHGYPID
AVVLTTGCDK TTPAGIMAAT TVNIPAIVLS GGPMLDGWHE GELVGSGTVI WRSRRKLAAG
EITEEEFIDR AASSAPSAGH CNTMGTASTM NAVAEALGLS LTGCAAIPAP YRERGQMAYK
TGQRIVDLAY EDVKPLDILT KKAFQNAIAL VAAAGGSTNA QPHIVAMARH AGVEITADDW
RAAYDIPLIV NMQPAGKYLG ERFHRAGGAP AVLWELLQQG RLHGDVLTVT GKTMGENLQG
RETSDREVIF PYHQPLAEKA GFLVLKGNLF DFAIMKSSVI GEEFRKRYLS EPGKEGVFEA
RAIVFDGSDD YHKRINDPAL EIDERCILVI RGAGPIGWPG SAEVVNMQPP DHLLKKGIMS
LPTLGDGRQS GTADSPSILN ASPESAIGGG LSWLRTGDTI RIDINTGRCD ALVDEATIAE
RKKEGIPAVP ATMTPWQEIY RAHTGQLESG GVLEFAVKYQ DLASKLPRHN H
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