ID DEOC_CLOBH Reviewed; 212 AA. AC A5I237; A7G3T9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 16-JUN-2009, entry version 17. 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=CBO1563, CLC_1594; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., RA Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T., RA Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., RA Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., RA Sanders M., Simmonds M., White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum RT strain Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). 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; CP000727; ABS38596.1; -; Genomic_DNA. DR EMBL; AM412317; CAL83102.1; -; Genomic_DNA. DR RefSeq; YP_001254070.1; -. DR RefSeq; YP_001387454.1; -. DR GeneID; 5185818; -. DR GeneID; 5400733; -. DR GenomeReviews; AM412317_GR; CBO1563. DR GenomeReviews; CP000727_GR; CLC_1594. DR KEGG; cbh:CLC_1594; -. DR KEGG; cbo:CBO1563; -. DR OMA; A5I237; 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; IPR011343; DeoC. DR InterPro; IPR002915; DeoC/AroFGH_arch. 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 1 212 Deoxyribose-phosphate aldolase. FT /FTId=PRO_1000057749. FT ACT_SITE 151 151 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 180 180 By similarity. SQ SEQUENCE 212 AA; 23060 MW; 4AC30E951CCFBDCB CRC64; MKLSKYIDHT LLKPQATEKD ILKLIEEAKT YDFASVCVNP SWVKLAYENL KDTDVKVCTV VGFPLGATST ASKVYETKVA IKDGADEIDM VISVGQLKSG NDEYVKEEIK KIVEASKNKL VKVIIETCLL TEEEKVKACT LSKEAGADYV KTSTGFSTGG AKPEDIKLMR ETVGKDMGVK ASGGIHTREE MEVMIENGAT RIGASCGVEL VK //