ID   R9K5Q1_9FIRM            Unreviewed;       581 AA.
AC   R9K5Q1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:EOS41734.1};
GN   ORFNames=C810_05257 {ECO:0000313|EMBL:EOS41734.1};
OS   Lachnospiraceae bacterium A2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=397290 {ECO:0000313|EMBL:EOS41734.1, ECO:0000313|Proteomes:UP000014150};
RN   [1] {ECO:0000313|EMBL:EOS41734.1, ECO:0000313|Proteomes:UP000014150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2 {ECO:0000313|EMBL:EOS41734.1,
RC   ECO:0000313|Proteomes:UP000014150};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium A2.";
RL   Submitted (APR-2013) 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:EOS41734.1}.
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DR   EMBL; ASSX01000042; EOS41734.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9K5Q1; -.
DR   STRING; 397290.C810_05257; -.
DR   PATRIC; fig|397290.3.peg.5803; -.
DR   eggNOG; COG0129; Bacteria.
DR   HOGENOM; CLU_014271_4_2_9; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000014150; 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:UP000014150}.
SQ   SEQUENCE   581 AA;  63192 MW;  162E83F7A2F54A89 CRC64;
     MELRSQEMRK LAPELDPLRI GTGWKPEDLL KPQVMIESTY GDSHPGSGHL NILVEEVRKG
     VEEAGGHGAR YYCTDICDGE SQGTDGINYS LASREMIANM IEIHANATPF DAGVFLASCD
     KGMPGNLMGL ARADVPSVVV PGGTMNAGPD MLTLEQLGMY NAKYQRGEID EEKLNWAKCN
     ACPSCGACSF IGTASTMQIM AEALGLALPG SALMPATSPD LLAFAREAGA QAVKLAAMPN
     MRPSHIITMD SFENAILVHA AISGSTNCLL HIPAIAHEFG LEVTGDTFDR LHRNARYLLD
     VRPAGRWPAE CFYYAGGVPA IMEEIKSHLH LEAMTVTGKT LGENLEELKQ NGFYGRCQKW
     LEDFNERYHV SLKKEDIIRP YGQAIGTDGS IAILRGNLAP EGAVIKHTAC PKEMFQAVLN
     ARPFDSEEEC LDAVLKHKVQ KGDAVFIRYE GPKGSGMPEM FYTSEAISSD KELGKSIALI
     TDGRFSGAST GPVIGHCSPE AVDCGPIALV EEGDLIEIDV EGRKLNIIGI AGERKTMEEV
     AAVLEERRKN WQPREPKYKN GVLRLFSQHA ASPMKGAYLE Y
//