ID   DEOC_SHEB5              Reviewed;         256 AA.
AC   A3D7J4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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}; OrderedLocusNames=Sbal_3227;
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) 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 = 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; CP000563; ABN62707.1; -; Genomic_DNA.
DR   RefSeq; WP_011847507.1; NC_009052.1.
DR   AlphaFoldDB; A3D7J4; -.
DR   SMR; A3D7J4; -.
DR   STRING; 325240.Sbal_3227; -.
DR   PRIDE; A3D7J4; -.
DR   EnsemblBacteria; ABN62707; ABN62707; Sbal_3227.
DR   KEGG; sbl:Sbal_3227; -.
DR   HOGENOM; CLU_053595_3_1_6; -.
DR   OMA; MNACIPP; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000001557; 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_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..256
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_1000072603"
FT   ACT_SITE        102
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
SQ   SEQUENCE   256 AA;  27393 MW;  ACBE0A16A310036E CRC64;
     MTDLKKAAQR AIELMDLTTL NDDDTDQKVI YLCHKAKTAA GNTAAICIYP RFIPIARKTL
     DEIGAEDIQI ATVTNFPHGN DDIAIAVLET RAAVAYGADE VDVVFPYRAL MEGNETIGFE
     LVKACKEACG EVLLKVIIES GVLADPALIR RASELSIDAG ADFIKTSTGK VPVNATLEAA
     EIMLTVISEK NTQVGFKPAG GVRDAAQAAE FLGVAERILG ADWVSPRTFR FGASSLLNSL
     LHTLELADAP KPTQGY