ID   DEOC_ECO5E              Reviewed;         259 AA.
AC   B5Z4R3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=ECH74115_5896;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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 = 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_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; CP001164; ACI39070.1; -; Genomic_DNA.
DR   RefSeq; WP_001295412.1; NC_011353.1.
DR   AlphaFoldDB; B5Z4R3; -.
DR   SMR; B5Z4R3; -.
DR   GeneID; 66671731; -.
DR   KEGG; ecf:ECH74115_5896; -.
DR   HOGENOM; CLU_053595_3_1_6; -.
DR   OMA; MNACIPP; -.
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: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_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   PANTHER; PTHR10889; PTHR10889; 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..259
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_1000129800"
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