ID A0A0F4RI85_9RHOB Unreviewed; 592 AA.
AC A0A0F4RI85;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KJZ18462.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KJZ18462.1};
GN ORFNames=TW80_13530 {ECO:0000313|EMBL:KJZ18462.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ18462.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ18462.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ18462.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ18462.1}.
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DR EMBL; JXYE01000006; KJZ18462.1; -; Genomic_DNA.
DR RefSeq; WP_045997971.1; NZ_JXYE01000006.1.
DR AlphaFoldDB; A0A0F4RI85; -.
DR STRING; 579483.TW80_13530; -.
DR PATRIC; fig|579483.3.peg.2771; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000033741; 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:KJZ18462.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033741}.
SQ SEQUENCE 592 AA; 63180 MW; C942D72F42045AF7 CRC64;
MSDSPPKRLR SQDWFANAER LDMTALYLER FMNYGLTPEE LRVGRPIIAI AQSGSDLSPC
NRIHLELEKR IRDGIRDAGG IALSFPTHPI FENCRRPTAA LDRNLAYLGL VEILNGYPID
GVVLTTGCDK TTPSALMAAL TVNIPAIVLN GGPMLNGWSG EERVGSGTVI WRARRALAAG
EIDERTFLDR AARSAPSAGH CNTMGTASTM NAVAEALGMA LTGAAAIPAP YRERGQMAYQ
SGKAAVDLVT SDIRPLDIIT PAALRNAIRI VSALGGSTNA QPHLTAIAAH AGHDLPTSAW
QDHGLRIPLL ANVQPAGAYL SEDFHRAGGV PAVMAELAKA GLLETDCLTV TGTSLADNLA
GHGSLNEEVI RSCDNPLSKS AGFIVMQGNF FDFAIMKASV ISNSFRTRFL SDPERPNCFT
ARVVVFDGAE DYHARINDPA LNIDETCILA MRNTGPLGWP GSAEVVNMQP PDQLIAAGIE
SLPSIGDGRQ SGTSDSPSIL HVSPEAALGG GLALLRDGDR LTVDLDRGRC DLDLSKEELA
ERAAKAGPKS IAPHTPWEKL FMENTTQLSE GMVLRDAPAM RNTSAKLPKH NH
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