ID   A1B8W9_PARDP            Unreviewed;       314 AA.
AC   A1B8W9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   01-MAY-2013, entry version 54.
DE   SubName: Full=Deoxyribose-phosphate aldolase;
DE            EC=4.1.2.4;
GN   OrderedLocusNames=Pden_3897;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 2 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between
CC       acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-
CC       D-ribose 5-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-
CC       glyceraldehyde 3-phosphate + acetaldehyde.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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DR   EMBL; CP000490; ABL71963.1; -; Genomic_DNA.
DR   RefSeq; YP_917659.1; NC_008687.1.
DR   ProteinModelPortal; A1B8W9; -.
DR   STRING; 318586.Pden_3897; -.
DR   EnsemblBacteria; ABL71963; ABL71963; Pden_3897.
DR   GeneID; 4582448; -.
DR   KEGG; pde:Pden_3897; -.
DR   PATRIC; 22858942; VBIParDen97112_3826.
DR   eggNOG; COG0274; -.
DR   HOGENOM; HOG000241644; -.
DR   KO; K01619; -.
DR   OMA; MVIDRGA; -.
DR   ProtClustDB; CLSK864118; -.
DR   UniPathway; UPA00002; UER00468.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:EC.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/lacD_aldolase.
DR   PANTHER; PTHR10889; PTHR10889; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   TIGRFAMs; TIGR00126; deoC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Lyase; Schiff base.
SQ   SEQUENCE   314 AA;  34073 MW;  45D167F10548563E CRC64;
     MERKNPGTDF RLDWFENIQV NTPAAERRAT SLAARRSLKK EWQAAWLLNA VRCIDLTTLS
     GDDTPDRVAR LCAKARQPVD AGQLAALGVE HLTTGAVCVY PTMVAAAKRA LRGTAIPVAS
     VATGFPAGLM PLDLRLAEIR YALDQGADEI DIVISRALVL RGEWAALYDE ICEMREACGS
     ARMKAILATG ELKTLTNVAR ASHVAMQAGA DFIKTSTGKE PVNATLPVSL VMLRAIRDYR
     DQTGFAVGFK PAGGLRTAKD ALNWQVLMAE ELGRDWLRPD LFRIGASSLL ADIERQISHH
     VTGRYAGAHR LAAG
//