ID A0A0F4RNR4_9RHOB Unreviewed; 580 AA.
AC A0A0F4RNR4;
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:KJZ21215.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KJZ21215.1};
GN ORFNames=TW80_00785 {ECO:0000313|EMBL:KJZ21215.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ21215.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ21215.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ21215.1,
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:KJZ21215.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXYE01000001; KJZ21215.1; -; Genomic_DNA.
DR RefSeq; WP_045995452.1; NZ_JXYE01000001.1.
DR AlphaFoldDB; A0A0F4RNR4; -.
DR STRING; 579483.TW80_00785; -.
DR PATRIC; fig|579483.3.peg.163; -.
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:KJZ21215.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033741}.
SQ SEQUENCE 580 AA; 62286 MW; F66FE1374FBC6F11 CRC64;
MTFTPAKWPR KLRSQEWYGG TSRDNIYHRG WLKNQGYPHD LFDGRPVIGI LNTWSELTPC
NGHLRELAEK VKAGVWEAGG FPVEVPVFSA SENTFRPTAM MYRNLAAMAV EEVMRAQPID
GAVLLVGCDK TTPSLMMGAA STDIPSIVVT GGPMLNGWFR GERVGSGTAL WQMSEDIKAG
KMTKEDFLEA EQAMSRSSGT CNTMGTASTM ASMAEALGMA LSGNAAIPGV DSRRKVMAQM
TGRRIVQMVK DDLKPSDIMT KQAFENAIRT NGAIGGSTNA VIHLLAMAGR VGVDLTLDDW
DRCGRDVPTI VNLMPSGKYL MEEFFYAGGL PVVLKRLGEA GLLHKDALTV SGGGIWDEVK
DATNWNEDVI LPVEKALAAS GGIAVLRGNL APKGAVLKPS AASPHLMKHR GRAVVFEDID
DYKAKINDDA LDIDESCVMV LKNCGPKGYP GMSEVGNMGL PPKVLKKGIT DMVRISDARM
SGTAYGTVVL HTAPEAAAGG PLAVVQNGDM IELDVAARRI HLDISEDELA TRLAAWSAPK
NAVVGGYSRL YLDHVEGADT GADFDVLKGQ RGNEVPRDSH
//