ID   DEOC_BURCC              Reviewed;         226 AA.
AC   B1KCV0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=Bcenmc03_6946;
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia cenocepacia MC0-3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000960; ACA96047.1; -; Genomic_DNA.
DR   RefSeq; WP_011545737.1; NC_010512.1.
DR   AlphaFoldDB; B1KCV0; -.
DR   SMR; B1KCV0; -.
DR   EnsemblBacteria; ACA96047; ACA96047; Bcenmc03_6946.
DR   KEGG; bcm:Bcenmc03_6946; -.
DR   HOGENOM; CLU_053595_0_1_4; -.
DR   OMA; KRGIGNE; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000002169; Chromosome 3.
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..226
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_1000094837"
FT   ACT_SITE        94
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        156
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        185
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   226 AA;  22887 MW;  887220CE40E78F49 CRC64;
     MPLSNAQLAQ TIDHTLLAPD ASDAQIRELC RQAAEHRFYS VCVNSANVPL AARELAETGV
     LVCAVVGFPL GAGLSAAKAF EATAAIAAGA GEIDMVINLG ALKSGRADDV KADIDAVHRA
     CGTVPLKVIL ETGLLTDDEK VRVCEMCRDL GVAFVKTSTG FGHGGATLAD VALMRRTVGP
     TLGVKASGGV RDRAAALAML EAGATRLGTS SGVAIVTDQG GGAAGY