ID   A0A3E1NFP9_9BACT        Unreviewed;       571 AA.
AC   A0A3E1NFP9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:RFM26793.1};
GN   ORFNames=DXN05_17540 {ECO:0000313|EMBL:RFM26793.1};
OS   Deminuibacter soli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Deminuibacter.
OX   NCBI_TaxID=2291815 {ECO:0000313|EMBL:RFM26793.1, ECO:0000313|Proteomes:UP000261284};
RN   [1] {ECO:0000313|EMBL:RFM26793.1, ECO:0000313|Proteomes:UP000261284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K23C18032701 {ECO:0000313|EMBL:RFM26793.1,
RC   ECO:0000313|Proteomes:UP000261284};
RA   Wang C.;
RT   "Chitinophagaceae sp. K23C18032701, a novel bacterium isolated from forest
RT   soil.";
RL   Submitted (AUG-2018) 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:RFM26793.1}.
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DR   EMBL; QTJU01000007; RFM26793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E1NFP9; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000261284; 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: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.
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:UP000261284}.
SQ   SEQUENCE   571 AA;  60835 MW;  D37B4B801AA0F049 CRC64;
     MEKTIRRSQG WFGRTGKDGF IYRAWMKKQG IAAHELQGKP VIGICNTWSE LTPCNSHFRE
     LAEAVKRGVL EAGGFPVEFP VMSLGETLIK PTAMLYRNLV SMDVEESIRA NPLDGVVLLC
     GCDKTTPALV MGACSVDLPT IVVSGGAMLT GRHEGRNIST SDIWRFSESV RSGKMTEEAL
     TLAEAGMCRS DGHCAVMGTA STMACMTEAL GISLPQNAAI PAPDAARKVL AQLSGSAIVR
     MVHEDVRLSH ILTREAFENA IKVNAAIGGS TNFAIHLLAI AARIGVQLSL EDIDTVAAGI
     PLLANLQPAG RYFMEDFYYA GGLPVVIKEL LPQLHAQCVT AAGATVQQIY EGCVNYNDEV
     IAGIQQPFNE VSGIMVLKGN LCENGAVIKP AAASAHLMQH TGRAVVFEDI DHYKALVDDP
     DLDVQANDIL VLKNVGPKGY PGMPEVGNMG LPAKLLAQGV TDMVRISDGR MSGTGFGTVV
     LHVSPEAAAG GTLAIVQTGD IITLDVPARK LEIALSAEEI AARKAQWQNA VKPAARGYVQ
     LYQQHVQQAH LGADFDFLQG GSGSEVSRDS H
//