ID X7F3W7_9RHOB Unreviewed; 580 AA.
AC X7F3W7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ETX27485.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:ETX27485.1};
GN ORFNames=RISW2_13740 {ECO:0000313|EMBL:ETX27485.1};
OS Roseivivax isoporae LMG 25204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX27485.1, ECO:0000313|Proteomes:UP000023430};
RN [1] {ECO:0000313|EMBL:ETX27485.1, ECO:0000313|Proteomes:UP000023430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX27485.1,
RC ECO:0000313|Proteomes:UP000023430};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX27485.1}.
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DR EMBL; JAME01000032; ETX27485.1; -; Genomic_DNA.
DR RefSeq; WP_043773644.1; NZ_JAME01000032.1.
DR AlphaFoldDB; X7F3W7; -.
DR STRING; 1449351.RISW2_13740; -.
DR PATRIC; fig|1449351.3.peg.3619; -.
DR eggNOG; COG0129; Bacteria.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000023430; 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:ETX27485.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000023430}.
SQ SEQUENCE 580 AA; 62466 MW; 065740ABEA257B75 CRC64;
MRFTPAPWPR RLRSQEWYGG TSRDHIYHRG WLKTQGYPHD LFDGRPVIGI LNTWSELTPC
NGHLRELAEK VKAGVWEAGG FPLEVPVFSA SENTYRPTAM MYRNLAAMAV EETLRAQPID
GAVLLVGCDK TTPSLMMGAA STDIPSIVVT GGPMLNGWFR GERVGAGTHL WKFSEAVKAG
EMTQEDFVEA EAAVTRSSGT CNTMGTASTM ASMAEALGMA LSGNAAIPAV DARRRVMAQL
SGRRIVQMVK DDLKPSDILT RAAFENAIRT NGAIGGSTNA VVHILALAGR AGVDLTLDDW
DRLGRDVPTI VNLMPSGQYL MEEFFYAGGL PVVLKRLGEA GLLNRDALTV SGGPIWDEVR
EARNWNEDVI LPVERALTAS GGIAVLRGNL APGGAVLKPS AASPELMVHR GRAVVFEDID
HYKARIADET LDIDETCVMV LKNCGPRGYP GMAEVGNMGL PQKVLRKGIT DMVRISDARM
SGTAYGTVVL HTSPEAARGG PLAVVRDGDM IELDVPARRL HLDIPDAELQ ARLEAWTPPA
PAPESGYARL FHAHVEGADT GADFDFLKGC RGAAVPKDSH
//
