ID A0A0X3W4A8_9ACTN Unreviewed; 584 AA.
AC A0A0X3W4A8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KUL50866.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KUL50866.1};
GN ORFNames=ADL30_28855 {ECO:0000313|EMBL:KUL50866.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL50866.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL50866.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL50866.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL50866.1}.
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DR EMBL; LLZK01000237; KUL50866.1; -; Genomic_DNA.
DR RefSeq; WP_062780495.1; NZ_LLZK01000237.1.
DR AlphaFoldDB; A0A0X3W4A8; -.
DR Proteomes; UP000053420; 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:KUL50866.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053420}.
SQ SEQUENCE 584 AA; 62493 MW; CDA1DC408A280835 CRC64;
MTGPAAERGG APRELRSSQW YGDGVSSGLR SFSHRARTRQ LGYLPEEHLG KPVIAVLNTW
SDINPCHSHL RDRAQAVKRG VWQAGGFPLE FPVSTLSETF QKPTPMLYRN LLAMETEELL
RSYPVDGAVL LGGCDKTTPA LLMGAASVDL PAVFVPAGPM LPGHWRGETL GSGTDMWKYW
DDHRAGLIGD CELTELESGL ARSPGHCMTM GTASTLTAAA EALGVTVPGA SSVPAVDSGH
DRMAAASGLR IVDLVRADRR LSHILTADAF EDAVTTVLGL GGSTNAVIHL IAMAGRAGVR
LTLDDFDRVA RTVPVLADVR PGGEKYLMED FHFAGGLPGF LSRITDLLHL DRPTVAHDSL
REQLAGARVH DEDVIRPRSN PVAGEGGVAV LRGNLCPDGA VIKHIAAEPR LLRHTGPAVV
FDDYRTMQRT IHDPSLGITP DHVLVLRGAG PKGGPGMPEY GMLPIPDYLL KQGVRDMVRI
SDARMSGTSY GACVLHVAPE SYVGGPLALV RTGDPVTLDV PGRTLHLGVD DAELARRRAE
WTPPPARYER GYGALYSEQI TQADTGCDFA FLARPGVVPD PYAG
//
