ID A5I1V1_CLOBH Unreviewed; 266 AA.
AC A5I1V1; A7G3K8;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000313|EMBL:CAL83015.1};
DE EC=2.5.1.55 {ECO:0000313|EMBL:CAL83015.1};
GN OrderedLocusNames=CBO1472 {ECO:0000313|EMBL:CAL83015.1};
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:CAL83015.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL83015.1, 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).
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DR EMBL; AM412317; CAL83015.1; -; Genomic_DNA.
DR RefSeq; WP_003358658.1; NC_009698.1.
DR RefSeq; YP_001253985.1; NC_009495.1.
DR RefSeq; YP_001387373.1; NC_009698.1.
DR AlphaFoldDB; A5I1V1; -.
DR SMR; A5I1V1; -.
DR GeneID; 5185727; -.
DR KEGG; cbh:CLC_1509; -.
DR KEGG; cbo:CBO1472; -.
DR PATRIC; fig|413999.7.peg.1452; -.
DR HOGENOM; CLU_062599_1_1_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IBA:GO_Central.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR GO; GO:0046364; P:monosaccharide biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006268; DAHP_syn_2.
DR NCBIfam; TIGR01361; DAHP_synth_Bsub; 1.
DR PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR PANTHER; PTHR43018:SF2; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001986};
KW Transferase {ECO:0000313|EMBL:CAL83015.1}.
FT DOMAIN 16..265
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 266 AA; 29878 MW; 118B861685498955 CRC64;
MEKLLIDKKN GENIRVKVGD IVIGGEEKII ISGPCAVEDE KTVVAIAENL KKLGVHMLRG
GAFKPRTSPY SFQGLKFEGL KILKECGKKF NMPIVSEVMD ARDLKEAYDY IDMIQIGSRN
MYNYTLLREV GKTKKPILLK RGMSATLNEW IYAAEYIMSE GNMNVVLCER GIRTFESYTR
NTLDLNTVAV IKDKYRVPII VDPSHATGFR EYVKPMSLAS IAGGADGLII ESHINPDNAI
SDARQTINVK EMKEIIDKVK QMDKIL
//
