ID   DEOC2_YERPS             Reviewed;         265 AA.
AC   Q66EW0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Deoxyribose-phosphate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=DERA 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00592};
DE   AltName: Full=Phosphodeoxyriboaldolase 2 {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=Deoxyriboaldolase 2 {ECO:0000255|HAMAP-Rule:MF_00592};
GN   Name=deoC2 {ECO:0000255|HAMAP-Rule:MF_00592}; OrderedLocusNames=YPTB0581;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19821.1; -; Genomic_DNA.
DR   RefSeq; WP_002216078.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66EW0; -.
DR   SMR; Q66EW0; -.
DR   EnsemblBacteria; CAH19821; CAH19821; YPTB0581.
DR   GeneID; 66842998; -.
DR   KEGG; ypo:BZ17_1978; -.
DR   KEGG; yps:YPTB0581; -.
DR   PATRIC; fig|273123.14.peg.2104; -.
DR   OMA; MNACIPP; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000001011; 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..265
FT                   /note="Deoxyribose-phosphate aldolase 2"
FT                   /id="PRO_0000231576"
FT   ACT_SITE        108
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        173
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        207
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
SQ   SEQUENCE   265 AA;  28274 MW;  353149B5782AEB14 CRC64;
     MTDLTACAHL NDYAKRALSL MDLTTLNDDD TDEKVIALCH QAKSPAGNTA AICIYPRFIP
     VARKALREQG TPEIRIATVT NFPHGNDDVA IALAETRAAI AYGADEVDVV FPYRALMAGN
     DKIGFELVKT CKEACAAANV LLKVIIETGE LKQAHLIRQA SEIAIKAGAD FIKTSTGKVP
     VNATLESADI MIRTIRELGV GETVGFKPAG GVRTAEDAAQ FLQLADQLMG EGWADARHFR
     FGASSLLASL LTTLGHQSNA NSSGY