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Database: UniProt
Entry: A0A261SEU5_9BORD
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Original site: A0A261SEU5_9BORD 
ID   A0A261SEU5_9BORD        Unreviewed;       585 AA.
AC   A0A261SEU5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:OZI35919.1};
DE            EC=4.2.1.9 {ECO:0000313|EMBL:OZI35919.1};
GN   ORFNames=CEG14_12805 {ECO:0000313|EMBL:OZI35919.1};
OS   Bordetella genomosp. 1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395607 {ECO:0000313|EMBL:OZI35919.1, ECO:0000313|Proteomes:UP000217005};
RN   [1] {ECO:0000313|EMBL:OZI35919.1, ECO:0000313|Proteomes:UP000217005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17610 {ECO:0000313|EMBL:OZI35919.1,
RC   ECO:0000313|Proteomes:UP000217005};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZI35919.1}.
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DR   EMBL; NEVL01000003; OZI35919.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SEU5; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000217005; Unassembled WGS sequence.
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:OZI35919.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   585 AA;  61816 MW;  B2AB7350B2C92835 CRC64;
     MDKKKDAKAP AAAPATGLKK GLTNYGDTGF SLFLRKAFIK GAGYTDSALD RPVIGIVNTG
     SSYNPCHGNA PQLIEAVKRG VMLAGGLPVD FPTISVHESF SQPTSMYLRN LMSMDTEEMI
     RAQPMDAVVL IGGCDKTVPA QLMGASSAGV PAIQLVTGSM LTGAHRGERV GACTDCRRYW
     GRYRAEEIDD VEIADVNNQL VASVGTCSVM GTASTMACLT EAMGMMVAGG ASAPAVTADR
     TRVAEQTGTT AVAMARARLT PDKILTGKAI ENALRVLLAI GGSTNGIVHM TAIAGRLGID
     IDLAGLDAMS RETPVLVDLK PSGQHYMEDF HKAGGMLALL RELRPLLHLD VMTVSGRTLG
     EELDAAPPPF KQDVIRPFDA PIYPVGGLAV LRGNLAPGGA IIKQSAANPK LMEHEGRAVV
     FESAEDMALR IDDPDLDVTA EDILVLKRIG PTGAPGMPEA GYMPIPKKLA VAGVKDMVRI
     SDGRMSGTAA GTIVLHVTPE SAIGGPLAYV QNGDRIRLSV KNREIALLIP DAELASRAAA
     APQERPSAER GYRKLFLQTV TQADQGVDFD FLRATETNEK VPRAR
//
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