ID A0A343JCK4_9CLOT Unreviewed; 571 AA.
AC A0A343JCK4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ASW43262.1};
GN ORFNames=BEN51_07130 {ECO:0000313|EMBL:ASW43262.1};
OS Clostridium isatidis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=182773 {ECO:0000313|EMBL:ASW43262.1, ECO:0000313|Proteomes:UP000264883};
RN [1] {ECO:0000313|EMBL:ASW43262.1, ECO:0000313|Proteomes:UP000264883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15098 {ECO:0000313|EMBL:ASW43262.1,
RC ECO:0000313|Proteomes:UP000264883};
RA Little G.T., Minton N.P.;
RT "Complete Genome Sequence Of The Indigo Reducing Clostridium isatidis
RT DSM15098.";
RL Submitted (AUG-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; CP016786; ASW43262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A343JCK4; -.
DR KEGG; cia:BEN51_07130; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000264883; Chromosome.
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:UP000264883}.
SQ SEQUENCE 571 AA; 62129 MW; 85E779E98CC6DFE0 CRC64;
MISQEIRKIA PEMDPLRRGM GYTSEDLSKV QIIIESTFGD SHPGSVHLLK FVNNAVKGVG
EKGGKASRFF ATDICDGMAQ GHDGINYSLA SRDALSNLIE IHANATPFDG GVFITSCDKG
VPAHLMAIGR INIPSIVVTG GVMKAGPNLL TLEQIGTYSA MERRGEITEE ELTYYKNNAC
PSAGSCSFMG TAATMQIMAE ALGLMLPGSS VMPANCEDLE KVAIEAGKQV VELAKKNLRA
RDIVTAKSFE NAIIIHAAIS GSSNSLLHIP AIAHEFGIEL DAEAFDKIHR YAPYLLNIRP
TGKWPAEYFY YAGGVPAIME ELKELLHLDV MTVTGKTLGE NLEDLKKNGY YEKCYEYLKE
TGLKKEDIIR PYTNPIGKNG AIAILRGNIA PDGAVVKHSA VPKEMHKAIL KARPFDSEEE
AIEAVLTKKI KPGDAVFIRY EGPKGSGMPE MFYTTEAISS DEELAASIAL ITDGRFSGAS
RGPAIGHVSP EAAEGGPIAL VEENDLIEID IENRILQMVG VNGERMPLEE IEKILNKRKE
SWKARKNKYE SGILKLYSDR AVSPMKGGYM E
//
