ID DEOC_BURCH Reviewed; 226 AA. AC A0KCV5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 16. 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=Bcen2424_6286; OS Burkholderia cenocepacia (strain HI2424). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 3 of Burkholderia cenocepacia RT HI2424."; RL Submitted (AUG-2006) 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 1 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; CP000460; ABK13018.1; -; Genomic_DNA. DR RefSeq; YP_839911.1; -. DR GeneID; 4454019; -. DR GenomeReviews; CP000460_GR; Bcen2424_6286. DR KEGG; bch:Bcen2424_6286; -. DR HOGENOM; A0KCV5; -. DR OMA; A0KCV5; AKMIDHT. 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_00114; -; 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 Complete proteome; Cytoplasm; Lyase; Schiff base. FT CHAIN 1 226 Deoxyribose-phosphate aldolase. FT /FTId=PRO_1000015310. FT ACT_SITE 156 156 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 185 185 By similarity. SQ SEQUENCE 226 AA; 22887 MW; 887220CE40E78F49 CRC64; MPLSNAQLAQ TIDHTLLAPD ASDAQIRELC RQAAEHRFYS VCVNSANVPL AARELAETGV LVCAVVGFPL GAGLSAAKAF EATAAIAAGA GEIDMVINLG ALKSGRADDV KADIDAVHRA CGTVPLKVIL ETGLLTDDEK VRVCEMCRDL GVAFVKTSTG FGHGGATLAD VALMRRTVGP TLGVKASGGV RDRAAALAML EAGATRLGTS SGVAIVTDQG GGAAGY //