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 16-JUN-2009, entry version 9. DE RecName: Full=Deoxyribose-phosphate aldolase; DE EC=4.1.2.4; DE AltName: Full=Phosphodeoxyriboaldolase; DE Short=Deoxyriboaldolase; DE Short=DERA; GN Name=deoC; OrderedLocusNames=EcolC_3675; OS Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=481805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., 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 -!- 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-D-ribose 1-phosphate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the deoC/fbaB aldolase family. DeoC type 2 CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000946; ACA79286.1; -; Genomic_DNA. DR RefSeq; YP_001726613.1; -. DR GeneID; 6066195; -. DR GenomeReviews; CP000946_GR; EcolC_3675. DR KEGG; ecl:EcolC_3675; -. DR OMA; B1IS38; CKEACGD. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:HAMAP. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:HAMAP. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro. DR HAMAP; MF_00592; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011343; DeoC. DR InterPro; IPR002915; DeoC/AroFGH_arch. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR PANTHER; PTHR10889; DeoC; 1. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF001357; DeoC; 1. DR TIGRFAMs; TIGR00126; deoC; 1. PE 3: Inferred from homology; KW Acetylation; Complete proteome; Cytoplasm; Lyase; Schiff base. FT CHAIN 1 259 Deoxyribose-phosphate aldolase. FT /FTId=PRO_1000082417. FT ACT_SITE 167 167 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 201 201 By similarity. FT MOD_RES 167 167 N6-acetyllysine (By similarity). 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 //