ID   A0A1Y6BD21_9PROT        Unreviewed;       580 AA.
AC   A0A1Y6BD21;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Dihydroxyacid dehydratase {ECO:0000313|EMBL:SME97738.1};
GN   ORFNames=SAMN05428998_102104 {ECO:0000313|EMBL:SME97738.1};
OS   Tistlia consotensis USBA 355.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Fodinicurvataceae; Tistlia.
OX   NCBI_TaxID=560819 {ECO:0000313|EMBL:SME97738.1, ECO:0000313|Proteomes:UP000192917};
RN   [1] {ECO:0000313|EMBL:SME97738.1, ECO:0000313|Proteomes:UP000192917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 355 {ECO:0000313|EMBL:SME97738.1,
RC   ECO:0000313|Proteomes:UP000192917};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
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DR   EMBL; FWZX01000002; SME97738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6BD21; -.
DR   STRING; 560819.SAMN05428998_102104; -.
DR   Proteomes; UP000192917; 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:UP000192917}.
SQ   SEQUENCE   580 AA;  62427 MW;  2DCB7D2FEEAAF8C2 CRC64;
     MSSKRDGRTG GYRSAEWFGP HDVHGVRHRN LMKNQGLPDD LFDGRPVIGI CNTYSELTPC
     NAHFRTLADR VKRGVWEAGG FPLEFPVTSL GETLMRPTAM LFRNLAAIDV EESIRANPVD
     GVVLLVGCDK TTPALVMGAA SCDLPTIAVS GGPMLSGHWR GETIGSGTHI WKFDAMVKAG
     EMTTADFLEA EGSIARSPGH CMTMGTASSM ASMVESLGLG LPQNAAIPAV DSRRNVLAHL
     AGRRIVEMVR QDLRLSKILT REAFENAVRT NGAIGGSTNA VVHLLAIAGR LKVDFTLDDW
     DRLGQGVPCL LDLMPSGRFL MEDFFYAGGL PVVLRRLGEA GLLNRDCVTA NGRSIWQNVE
     TAQCWNDEVI RPFDKPAKPQ GGIAVLRGSL APDGAVIKPS AASPELMQHR GRAVVFEDIE
     DYRARCDDPD LPLEPGSILV LKNCGPVGYP GMPEVGNMRL PERMLKAGVR DMVRISDARM
     SGTAFGTVVL HAAPEAAVGG PLALVETGDE IELDVAGRRL DLLVGGEELA RRRAAWRPSH
     PVADRGWVRL YQETVNQADK GADLGFLTGG SGAPIPRESH
//