ID A5HYI4_CLOBH Unreviewed; 571 AA.
AC A5HYI4; A7G0J0;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Probable dehydratase {ECO:0000313|EMBL:CAL81843.1};
GN OrderedLocusNames=CBO0291 {ECO:0000313|EMBL:CAL81843.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL81843.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL81843.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; AM412317; CAL81843.1; -; Genomic_DNA.
DR RefSeq; WP_011948081.1; NC_009698.1.
DR RefSeq; YP_001252834.1; NC_009495.1.
DR RefSeq; YP_001386245.1; NC_009698.1.
DR AlphaFoldDB; A5HYI4; -.
DR GeneID; 5184546; -.
DR KEGG; cbh:CLC_0350; -.
DR KEGG; cbo:CBO0291; -.
DR PATRIC; fig|413999.7.peg.291; -.
DR HOGENOM; CLU_014271_4_2_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
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; 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:UP000001986}.
SQ SEQUENCE 571 AA; 61966 MW; B014C2A900C457DA CRC64;
MISQDIRKIA PEMDPLRRGM GWSVEDLSKP QIIVESTFGD SHPGSAHLIK FANNAVQGVA
ERGGKAARYF ATDICDGMAQ GHDGINYSLA SRDTITSLIE IHANATPFDG GVFISSCDKA
VPSHLMAIGR LNIPSIVVTG GVMEAGPNLL TLEQIGAYSA MYQRKEITEE ELTYYKHNAC
PSCGACSFMG TASTMQVMAE ALGLMLPGSA LMPATCKDLE DVAVEAGKQV VELAKMNLKP
KDIVTEKSFE NAIIIHAAIS GSTNSLLHIP AIAHEFGIKI DEESFDRIHR YAPYLLNIRP
AGKWPAEYFY YAGGVPAIME EVKHLLHLDV MTVTGKTLGE NLEDLKKNGY YKNCDKYLKK
VGLTRRDVIK PISEPIGENG AIAILKGNIA PEGAVVKHSA VPEEMHKGIL KARPFDSEEE
AISAIISKKI NPGDAVFIRY EGPKGSGMPE MFYTTEAISS DKELSASIAL ITDGRFSGAS
KGPAIGHVSP EAAMGGPIAL VEENDLIEID IEKRILQLVG VNGQKLSEEA IDKVLVERKA
KWEKRENKYK SGILKIFSER AVSPMKGGYM E
//
