ID   A0A0W1DT55_9SPHN        Unreviewed;       593 AA.
AC   A0A0W1DT55;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KTE21129.1};
DE            EC=4.2.1.9 {ECO:0000313|EMBL:KTE21129.1};
GN   ORFNames=ATE67_07350 {ECO:0000313|EMBL:KTE21129.1};
OS   Sphingopyxis sp. H050.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE21129.1, ECO:0000313|Proteomes:UP000053439};
RN   [1] {ECO:0000313|Proteomes:UP000053439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA   Gomez-Alvarez V., Revetta R.P.;
RL   Submitted (NOV-2015) 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:KTE21129.1}.
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DR   EMBL; LNRZ01000003; KTE21129.1; -; Genomic_DNA.
DR   RefSeq; WP_058816082.1; NZ_LNRZ01000003.1.
DR   AlphaFoldDB; A0A0W1DT55; -.
DR   STRING; 1759072.ATE67_07350; -.
DR   Proteomes; UP000053439; 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   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; 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.
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:KTE21129.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   593 AA;  64591 MW;  7CA6137EF6403C08 CRC64;
     MTTPPPRPRL RSRDWFDNPE RWDMTALYLE RFMNYGTTPE ELQSGKPIIG IAQSGSDLSP
     CNRVHVDLAK RVRDGIRDAG GIPIEFPVHP IFENCRRPTA ALDRNLAYLA LVEILNGYPL
     DAVVLTTGCD KTTPSQVMAA TTVDIPAIVL SGGPMLDGWH DGELVGSGTV IWRSRRALSA
     GLIDEAEFLG RATSSAPSLG HCNSMGTAST MNAVAEALGL SLTGCAAIPA PYRERGQYAY
     RTGRRIVEMV HEDLRPSRIL TREAFLNAIA TVSVCGGSSN AQPHIVAMAR HAGVELEPDI
     WSEHGYDLPL LVNMQPAGQY LGERFHRAGG VPAAMWELLN AGKLFGDCLT VTGRSIADNL
     AGQESADREM IRPFADPLQA KAGFLTLKGN LFDFAVMKTS VISDEFRQRY LSRPGAEGVF
     EARAVVFDGS DDYHHRINDP ALDIDENCIL VMRSSGILGW PGSAEVVNMQ PPDALIQRGI
     QWLPTLGDGR QSGTSDSPSI LNASPESAAG GGLAWLRDGD MIRIDLNAGT CDMLVDADEI
     ERRKADGLPE IPPSNTPWEE LFREKTGQLG EGGVMEFALK YRQTSRQLPR HNH
//