ID   A0A0L0JJE2_9ACTN        Unreviewed;       570 AA.
AC   A0A0L0JJE2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KND25728.1};
DE            EC=4.2.1.9 {ECO:0000313|EMBL:KND25728.1};
GN   ORFNames=IQ63_40310 {ECO:0000313|EMBL:KND25728.1};
OS   Streptomyces acidiscabies.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=42234 {ECO:0000313|EMBL:KND25728.1, ECO:0000313|Proteomes:UP000037151};
RN   [1] {ECO:0000313|Proteomes:UP000037151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA   Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT   "Genome sequencing of plant-pathogenic Streptomyces species.";
RL   Submitted (JUL-2014) 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:KND25728.1}.
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DR   EMBL; JPPY01000218; KND25728.1; -; Genomic_DNA.
DR   RefSeq; WP_050375031.1; NZ_KQ257834.1.
DR   AlphaFoldDB; A0A0L0JJE2; -.
DR   PATRIC; fig|42234.21.peg.8296; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000037151; 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:KND25728.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037151}.
SQ   SEQUENCE   570 AA;  60175 MW;  33912D40BF6AA867 CRC64;
     MTLRSAQWYE GQDRNAYIHR AWMRRGVPDD AFTGRPQIAI ANTASDLTPC NAHLDEVAAS
     VRNGVYEAGG IPLDLPVVSL GETQVRPTAM LWRNMAAMAT EEMLRANPID GVVLLGGCDK
     TIPSLLMAAA SVDLPAVVVP GGPMLNGTFQ GALLGCGTGV WKLSEEVRAG TLSQADFTRS
     ESAMIRSKGH CNTMGTASTM ALVAEALGTV VPGVAGTPAP DSRLLQAAHG TGKLAVEMVA
     ADRRPGTFLT KASFHNAIVA LAAIGGSTNA VVHLLAIAGR LGIDLTLDDF DRVGSRVPVL
     VDLQPAGRYL MEDFHRAGGL LAVLREVQDL LDPTALTVTG TPLVSYLSDA AIWDAEVIRS
     RTEPLVAEGG IAVLRGNLAP DGALLKPAAA SPHLLQHRGR AVVFDSVEDF HARIDDPDLD
     VDADSILVLR GCGPKGYPGM PEVANMPLPK KLLAQGIRDM VRICDGRMSG TAYGTVVLHV
     APEAAAGGPL ALVRTGDIIE LDVPSRRITL DVPEPELSRR EPTKTTTAAF ASPHRGWERL
     YIDHVLQADT GADLDFLVGS SGSEVSRESH
//