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
//