ID Q2T4S3_BURTA Unreviewed; 583 AA.
AC Q2T4S3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ABC35951.1};
GN OrderedLocusNames=BTH_II1632 {ECO:0000313|EMBL:ABC35951.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC35951.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC35951.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP000085; ABC35951.1; -; Genomic_DNA.
DR RefSeq; WP_009897564.1; NZ_CP008786.1.
DR AlphaFoldDB; Q2T4S3; -.
DR KEGG; bte:BTH_II1632; -.
DR HOGENOM; CLU_014271_3_1_4; -.
DR Proteomes; UP000001930; Chromosome II.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 583 AA; 62055 MW; 929DA49E8BA08960 CRC64;
MSASKPKLRS AQWFGTHDKN GFMYRSWMKN QGIPDHEFDG RPIVGICNTW SELTPCNAHF
RKLAEHVKRG VYEAGGFPVE FPVFSNGESN LRPSAMLTRN LASMDVEEAI RGNPIDAVVL
LAGCDKTTPA LLMGAASCDV PAIVVSGGPM LNGKLDGKNI GSGTAVWQLH EALKAGEIDL
HRFLSAEAGM SRSAGTCNTM GTASTMACLA EALGVALPHN AAIPAVDARR YVLAHMSGMR
IVGMAHEGLV LSKILTRAAF ENAIRVNAAI GGSTNAVIHL KAIAGRLGVP LELEDWLRLG
RGTPTIVDLM PSGRFLMEEF YYAGGLPAVL RRLGEANLLP HPGALTVNGQ SLWDNVRDAP
SHDDEVIRPL DRPLIADGGI RILRGNLAPR GAVLKPSAAS PELLKHRGRA VVFENFEHYK
ATIDDEALDV DANSVLVLKN CGPRGYPGMA EVGNMGLPPK LLRQGVKDMV RISDARMSGT
AYGTVVLHVA PEAAAGGPLA AVRNGDWIEL DGEAGTLTLD VSDDELARRL SDHDPASAPG
VAEHAAGGGY ARLYVDHVLQ ADEGCDLDFL VGRRGAAVPR HSH
//
