ID   A0A1M4TXP4_9CLOT        Unreviewed;       574 AA.
AC   A0A1M4TXP4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:SHE49216.1};
GN   ORFNames=SAMN02745158_00625 {ECO:0000313|EMBL:SHE49216.1};
OS   Lactonifactor longoviformis DSM 17459.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Lactonifactor.
OX   NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE49216.1, ECO:0000313|Proteomes:UP000184245};
RN   [1] {ECO:0000313|EMBL:SHE49216.1, ECO:0000313|Proteomes:UP000184245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE49216.1,
RC   ECO:0000313|Proteomes:UP000184245};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQVI01000002; SHE49216.1; -; Genomic_DNA.
DR   RefSeq; WP_072848922.1; NZ_FQVI01000002.1.
DR   AlphaFoldDB; A0A1M4TXP4; -.
DR   STRING; 1122155.SAMN02745158_00625; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000184245; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; 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; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-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.
DR   PROSITE; PS00887; ILVD_EDD_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
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:ARBA00022714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184245}.
SQ   SEQUENCE   574 AA;  62080 MW;  6AE0A96FCBE50877 CRC64;
     MSNIQQKSAP QRLYWAQLDA LNMGSGWDEE DITKPQILLE DVYGDSHPGS THLSQLMEQA
     KYGVFERGGF PAQYHTTDIC DGCAQGHDGM NYVLASREAI CDMVEVHGSV YPWDGMILAS
     SCDKSIPAHL KAAARLNIPT IFIPGGSMRP GPNMTTSLVA GDISLRQKRE GEISDQEVRD
     YKLTGCPSCG ACTFLGTAST MQCMAEALGM ALPGSAVMPA TMRDIQSYAR KAGRAIMGLV
     EKDIKPGDIM TEAAFRNAVI IHSAIGGSTN ATLHLPSIAR EMSLELSPDL FDEINHRVPH
     LGNITPSGQH LTEAFWFAGG IPMVQWYLKD MLDLDVMTVT GKPLGENLEM LAKENFFERN
     LGYLSNYGLT RDEVIFPVEK AEEKGSIAIL KGNLAPEGSV VKYSACVKEL RIHKGTARVY
     NREEDAYQAV VDGKINPGDV VVIRYEGPRG TGMPEMLMTT EAIVCDERLN GTVSLVTDGR
     FSGATRGAAI GHVSPEAACG GPLAFIETGD IISYNIPERT IDVVGINGEE MSPAEVGKIL
     DERSKRGIIP SPRRSGLFGR YTSSALSAMK GAGY
//