ID A0A1B2R6L3_9BORD Unreviewed; 598 AA.
AC A0A1B2R6L3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AOB32621.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:AOB32621.1};
GN ORFNames=AKI39_20585 {ECO:0000313|EMBL:AOB32621.1};
OS Bordetella sp. H567.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB32621.1, ECO:0000313|Proteomes:UP000093512};
RN [1] {ECO:0000313|Proteomes:UP000093512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) 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; CP012334; AOB32621.1; -; Genomic_DNA.
DR RefSeq; WP_066640357.1; NZ_CP012334.1.
DR AlphaFoldDB; A0A1B2R6L3; -.
DR STRING; 1697043.AKI39_20585; -.
DR KEGG; boh:AKI39_20585; -.
DR PATRIC; fig|1697043.4.peg.4213; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000093512; 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:AOB32621.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000093512}.
FT REGION 572..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 63057 MW; B3B923432060FBA3 CRC64;
MSSKSSSTSD AAAASGMRKG LTSYGDAGFS LFLRKAFIKG AGLSDDALSR PIVGIANTGS
GFNPCHGNMP QLLEAVKRGV MLAGGLPVEF PTISVHESFA SPTSMFLRNL MSMDTEEMIR
AQPMDAVVLI GGCDKTVPAQ LMAAASGKVP AIQLVTGSML TGSHRGERVG ACTDCRRFWG
KYRAEEIDDA EIADVNNQLV ASVGTCSVMG TASTMACIAE ALGIAVPGSA SPPAVTADRI
RVAERTGAEA VAMIGRQLTP DRILTAKSFE NALRVLLAIG GSTNGIVHLT AVAGRLGIAL
DMEAFDRIGK ETPVLVDLKP SGQHYMEDFH KAGGVRTLLR ELRPLLHLDA LTVTGRTLGE
ELDDAPPAFP QDVVRPFDKP VYAQGGIAVL RGNLAPGGAI IKQSAATAAL MEHEGRAVVF
EDLEDLAARV DDEELDIHAD DIMVLKHIGP VGAPGMPEAG YMPIPRKLAR AGVKDMVRIS
DGRMSGTASG SIVLHVTPES AIGGPLALVR TGDRIRLSVQ RREISLLVDD AELARRKAAW
RPRPAREGDD RGYRKLFLST VTQADKGCDF DFLRGTQDNG STPIGKPPAS GGQAAKKP
//
