ID DEOC_CLOK5 Reviewed; 218 AA. AC A5N0Z3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 16-JUN-2009, entry version 19. 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=CKL_2777; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., RA Hagemeier C., Thauer R.K., Gottschalk G.; RT "The genome of Clostridium kluyveri, a strict anaerobe with unique RT metabolic features."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008). 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; CP000673; EDK34789.1; -; Genomic_DNA. DR RefSeq; YP_001396160.1; -. DR GeneID; 5392484; -. DR GenomeReviews; CP000673_GR; CKL_2777. DR KEGG; ckl:CKL_2777; -. DR NMPDR; fig|431943.4.peg.2826; -. DR OMA; A5N0Z3; 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 1 218 Deoxyribose-phosphate aldolase. FT /FTId=PRO_1000076028. FT ACT_SITE 155 155 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 184 184 By similarity. SQ SEQUENCE 218 AA; 23545 MW; A47504B5AB52B1CB CRC64; MDKKELAKMI DHTLLKPEAN YEQIVKLCKE ALEYGFASVC INPCYVNAAY QLLKGSDVKV CTVVGFPLGA ATSETKTFEA VQAVNRGASE IDMVINVGYL KSGNHDYVEE DIKTLVNKIN GRALVKVIIE TCLLNDEEKI IACKLAKKAG AHFVKTSTGF NMSGATSEDV ALMYDAVSPN LKVKASGGIR TYEDAIKMIN AGASRIGASS SIKIINKK //