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Database: UniProt
Entry: A0A0F4RNR4_9RHOB
LinkDB: A0A0F4RNR4_9RHOB
Original site: A0A0F4RNR4_9RHOB 
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}.
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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
//
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