DEOC_BACC0
ID DEOC_BACC0 Reviewed; 223 AA.
AC B7JJK4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=BCAH820_1927;
OS Bacillus cereus (strain AH820).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-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; CP001283; ACK87218.1; -; Genomic_DNA.
DR RefSeq; WP_001017446.1; NC_011773.1.
DR AlphaFoldDB; B7JJK4; -.
DR SMR; B7JJK4; -.
DR EnsemblBacteria; ACK87218; ACK87218; BCAH820_1927.
DR GeneID; 45021821; -.
DR KEGG; bcu:BCAH820_1927; -.
DR HOGENOM; CLU_053595_0_1_9; -.
DR OMA; MNACIPP; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000001363; 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..223
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_1000117539"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 152
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ SEQUENCE 223 AA; 23411 MW; 2A98ABB54B10BA39 CRC64;
MNIAKLIDHT ILKANTTKED VMKVIEEAKE YKFASVCINP TWVKLAAEEL AGHDVDVCTV
IGFPLGASTT ETKAFETKDA IAKGATEVDM VINVGALKDG DNELVEKDIY EVVQAAKGKA
LVKVIIETCL LTDEEKVRAC ELSVKAGADF VKTSTGFSTG GATAEDIALM RKTVGPNVGV
KASGGVRTRE DAEKMVAAGA SRVGASASVA IVLNDAKGAT DNY
