ID DEOC1_OCEIH Reviewed; 221 AA. AC Q8EPW8; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 44. DE RecName: Full=Deoxyribose-phosphate aldolase 1; DE EC=4.1.2.4; DE AltName: Full=Phosphodeoxyriboaldolase 1; DE Short=Deoxyriboaldolase 1; DE Short=DERA 1; GN Name=deoC1; Synonyms=dra; OrderedLocusNames=OB1963; OS Oceanobacillus iheyensis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus. OX NCBI_TaxID=182710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831; RX MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya RT Ridge and its unexpected adaptive capabilities to extreme RT environments."; RL Nucleic Acids Res. 30:3927-3935(2002). 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; BA000028; BAC13919.1; -; Genomic_DNA. DR RefSeq; NP_692884.1; -. DR HSSP; Q9X1P5; 1O0Y. DR GeneID; 1018440; -. DR GenomeReviews; BA000028_GR; OB1963. DR KEGG; oih:OB1963; -. DR NMPDR; fig|221109.1.peg.1963; -. DR HOGENOM; Q8EPW8; -. DR OMA; Q8EPW8; AKMIDHT. DR BioCyc; OIHE221109:OB1963-MON; -. DR BRENDA; 4.1.2.4; 278212. 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 1 221 Deoxyribose-phosphate aldolase 1. FT /FTId=PRO_0000057250. FT ACT_SITE 152 152 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 181 181 By similarity. SQ SEQUENCE 221 AA; 23666 MW; 81E76D434976E093 CRC64; MDLAKYIDHT QLKPDTTKQS IVKIVEEAKQ HEFASVCVNP HWVSYCYNEL KDTPVKVCTV IGFPLGATST ETKIFETNQA IADGATEVDM VINVGELKSN NDAFVEKDIR AVVEAAKGKA LTKVIIETSL LTEDEKVRAC KLAKNAEADY VKTSTGFSGG GATVEDIRLM RETVGPEMGV KASGGVRDLE QTEAMIEAGA TRIGASSGVA IVSGEQGTSD Y //