ID DEOC_BACA2 Reviewed; 222 AA. AC A7ZAF1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 12. 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=RBAM_036480; OS Bacillus amyloliquefaciens (strain FZB42). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(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; CP000560; ABS75977.1; -; Genomic_DNA. DR RefSeq; YP_001423208.1; -. DR GeneID; 5459960; -. DR GenomeReviews; CP000560_GR; RBAM_036480. DR KEGG; bay:RBAM_036480; -. DR OMA; A7ZAF1; 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 1 222 Deoxyribose-phosphate aldolase. FT /FTId=PRO_1000015308. FT ACT_SITE 152 152 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 181 181 By similarity. SQ SEQUENCE 222 AA; 22897 MW; E71D4DAD17178547 CRC64; MSIASQIDHT ALKPHTQKAD ILQLIKEAKE YKFASVCVNP TWVKLAAEEL KGTGVDVCTV IGFPLGATTS ETKAFETKDA ISKGATEVDM VINIGALKDG DDEAVEADIR AVVEAADKKA LVKVIIETCL LTDEEKERAC RLAVSAGADF VKTSTGFSTG GATAEDIALM RKTVGPDIGV KASGGIRTKA DVDSMIAAGA SRIGASAGVS IVSGGDSGSS DY //