ID   DEOC_CLOBK              Reviewed;         212 AA.
AC   B1ILA1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114};
DE            EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
GN   Name=deoC {ECO:0000255|HAMAP-Rule:MF_00114}; OrderedLocusNames=CLD_2989;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC       and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00114};
CC   -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC       degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC       deoxy-alpha-D-ribose 1-phosphate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00114}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00114}.
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DR   EMBL; CP000939; ACA45338.1; -; Genomic_DNA.
DR   RefSeq; WP_004451714.1; NC_010516.1.
DR   AlphaFoldDB; B1ILA1; -.
DR   SMR; B1ILA1; -.
DR   EnsemblBacteria; ACA45338; ACA45338; CLD_2989.
DR   KEGG; cbb:CLD_2989; -.
DR   HOGENOM; CLU_053595_0_1_9; -.
DR   OMA; MNACIPP; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00959; DeoC; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00114; DeoC_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR028581; DeoC_typeI.
DR   PANTHER; PTHR10889; PTHR10889; 1.
DR   PANTHER; PTHR10889:SF1; PTHR10889:SF1; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   TIGRFAMs; TIGR00126; deoC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Schiff base.
FT   CHAIN           1..212
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_1000094841"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        151
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        180
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   212 AA;  23122 MW;  0FB325FD88F9D43D CRC64;
     MKLSKYIDHT LLKPQATEKD ILKLIEEAKT YDFASVCVNP SWVKLAYENL KDTDVKVCTV
     VGFPLGATST ASKVYETKVA IEDGADEIDM VISVGQLKSG NDEYVKEEIK KIVEASKNRL
     VKVIIETCLL TEEEKVKACT FSKEAGADYV KTSTGFSTGG AKPEDIKLMR ETVGKNMGVK
     ASGGIHTREE MEVMIENGAT RIGASCGVEL VK