ID A0A0W7WIF2_9RHOB Unreviewed; 576 AA.
AC A0A0W7WIF2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KUF10318.1};
GN ORFNames=AVJ23_13000 {ECO:0000313|EMBL:KUF10318.1};
OS Pseudoponticoccus marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoponticoccus.
OX NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF10318.1, ECO:0000313|Proteomes:UP000054396};
RN [1] {ECO:0000313|EMBL:KUF10318.1, ECO:0000313|Proteomes:UP000054396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF10318.1,
RC ECO:0000313|Proteomes:UP000054396};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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:KUF10318.1}.
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DR EMBL; LPXO01000007; KUF10318.1; -; Genomic_DNA.
DR RefSeq; WP_058862636.1; NZ_LPXO01000007.1.
DR AlphaFoldDB; A0A0W7WIF2; -.
DR STRING; 1685382.AVJ23_13000; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000054396; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054396}.
SQ SEQUENCE 576 AA; 62402 MW; 75F0226928BCE060 CRC64;
MTKSYEDLRS ARWFAPDDLR SMGHRSRAMQ MGLSGDDWEG KPIIAIINTW SDLSPCHHHL
RDRAEFVKKG VYQAGGMPVE MPVHSFSEQF LKPTSMLYRN MGAIEVEETL RSHPIDGVVL
MGGCDKSTPA LVMGAASMGL PFIYLPAGAM LRGNYAGQKL GSGTDVWKYW DERRAGTIGK
AEWDGVQGGI ARSYGTCMTM GTASTMMSIA DGWGLTLPGA SSIPAPDAGH KRMSAACGRR
IVEMVWEDLT PDRIMTPAST RNAVTVAMAT GCSTNAIIHL IAMARRAGVP LELDDLDAIG
RTTPVLANLR PSGSEYLMED FFYAGGLPAL MTELGDKLDL SVMTVTGKTL GENIAGAQTF
NDDVIRPLSN PVYHEGSLAV LKGNLAPDGA VIKPAAMDAR FQTHAGPAIV ADSYAQLKEI
INDEDYPMTP DSVMVLRNAG PQGGPGMPEW GMIPMPKALL KQGHRDMVRL SDARMSGTSY
GACILHVAPE AFVGGPLALI ETGDIIELDI PNRSLNVRLS EEELAARRAA WTPPAPRFER
GYGWMFSRHI EQADKGCDFD FLRTEFGAPV PEPEIN
//
