ID A0A0M8YY65_9ACTN Unreviewed; 579 AA.
AC A0A0M8YY65;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KOX45933.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KOX45933.1};
GN ORFNames=ADL09_20590 {ECO:0000313|EMBL:KOX45933.1};
OS Streptomyces sp. NRRL F-7442.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX45933.1, ECO:0000313|Proteomes:UP000037772};
RN [1] {ECO:0000313|EMBL:KOX45933.1, ECO:0000313|Proteomes:UP000037772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX45933.1,
RC ECO:0000313|Proteomes:UP000037772};
RA Noorani M.;
RL Submitted (JUL-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:KOX45933.1}.
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DR EMBL; LGEH01000154; KOX45933.1; -; Genomic_DNA.
DR RefSeq; WP_030403804.1; NZ_LGEH01000154.1.
DR AlphaFoldDB; A0A0M8YY65; -.
DR PATRIC; fig|1519498.3.peg.4279; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000037772; 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:SF2; DIHYDROXY-ACID DEHYDRATASE; 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:KOX45933.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 579 AA; 62479 MW; 1D7A20E41EAC1CD6 CRC64;
MTAPAGRKAP EQLRSHQWYG TDGLRSFSHR ARTRQLGYLP EEHLGKPVIA ILNTWSDINP
CHVHLRDRAQ AVKRGVWQAG GFPLEFPVST LSETFQKPTP MLYRNLLAME TEELLRSYPV
DGAVLMGGCD KSTPALLMGA ASVDLPAVFV PAGPMLPGHW RGQTLGSGTD MWKYWDDKRA
GLIGDCEMQE LESGLARSPG HCMTMGTAST LTAAAEALGV TVPGASSIPA VDSGHDRMAA
AAGLRIVELV HRDRKLSDIL TADAFEDAVT TVLGLGGSTN AVIHLIAMAG RAGVTLTLDD
FDRIARTVPV LANVRPGGQT YLMEDFHFAG GLPGFLSRIT DLLHLDRPTV SHDTLREQLD
GALVHHDDVI RPRDNPVASE GGVAVLRGNL CPDGAVIKHI AAEPHLLKHT GPAVVFDDYK
TMQRTINDPE LGITADSVLV LRNAGPKGGP GMPEYGMLPI PDHLLKQGVR DMVRISDARM
SGTSYGACVL HVAPESYVGG PLALVRTGDS ITLDVEARSL RLDVDDEELE RRRAAWTPPP
ARYERGYGAL YNEQITQADT GCDFEFLARP GTVQDPYAG
//
