ID   DEOC_ECOLC              Reviewed;         259 AA.
AC   B1IS38;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   28-JAN-2026, entry version 90.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=DERA {ECO:0000255|HAMAP-Rule:MF_00592};
DE            EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00592};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
GN   Name=deoC {ECO:0000255|HAMAP-Rule:MF_00592};
GN   OrderedLocusNames=EcolC_3675;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 /
RC   Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
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_00592}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate +
CC         acetaldehyde; 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_00592};
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_00592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00592}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00592}.
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DR   EMBL; CP000946; ACA79286.1; -; Genomic_DNA.
DR   RefSeq; WP_001295412.1; NC_010468.1.
DR   PDB; 9FD7; X-ray; 1.40 A; A/B=1-259.
DR   PDB; 9FD8; X-ray; 1.58 A; A/B=1-259.
DR   PDB; 9FD9; X-ray; 1.52 A; A/B=1-259.
DR   AlphaFoldDB; B1IS38; -.
DR   SMR; B1IS38; -.
DR   GeneID; 86944916; -.
DR   GeneID; 93777463; -.
DR   KEGG; ecl:EcolC_3675; -.
DR   HOGENOM; CLU_053595_3_1_6; -.
DR   UniPathway; UPA00002; UER00468.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006018; P:2-deoxyribose 1-phosphate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:TreeGrafter.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   CDD; cd00959; DeoC; 1.
DR   FunFam; 3.20.20.70:FF:000034; Deoxyribose-phosphate aldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00592; DeoC_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR023649; DeoC_typeII.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PDBsum; 9FD7; -.
DR   PDBsum; 9FD8; -.
DR   PDBsum; 9FD9; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lyase; Schiff base.
FT   CHAIN           1..259
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_1000082417"
FT   ACT_SITE        102
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        167
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        201
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
SQ   SEQUENCE   259 AA;  27748 MW;  3D7EA7C83DE4124F CRC64;
     MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL
     KEQGTPEIRI ATVTNFPHGN DDIEIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD
     LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE
     SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL
     LASLLKALGH GDGKSASSY
//