ID DEOC_THEMA Reviewed; 248 AA. AC Q9X1P5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 25-NOV-2008, entry version 67. 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=TM_1559; OS Thermotoga maritima. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=2336; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX MEDLINE=99287316; PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). 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; AE000512; AAD36625.1; -; Genomic_DNA. DR PIR; B72240; B72240. DR RefSeq; NP_229359.1; -. DR PDB; 1O0Y; X-ray; 1.90 A; A/B=1-248. DR PDBsum; 1O0Y; -. DR GeneID; 897566; -. DR GenomeReviews; AE000512_GR; TM_1559. DR KEGG; tma:TM1559; -. DR NMPDR; fig|243274.1.peg.1543; -. DR TIGR; TM_1559; -. DR HOGENOM; Q9X1P5; -. DR BioCyc; TMAR243274:TM_1559-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Lyase; Schiff base. FT CHAIN 1 248 Deoxyribose-phosphate aldolase. FT /FTId=PRO_0000057280. FT ACT_SITE 179 179 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 208 208 By similarity. FT HELIX 1 16 FT STRAND 22 24 FT HELIX 28 34 FT STRAND 35 39 FT HELIX 46 59 FT STRAND 62 66 FT HELIX 68 70 FT HELIX 71 78 FT STRAND 84 90 FT TURN 91 93 FT HELIX 98 111 FT STRAND 114 119 FT HELIX 122 126 FT HELIX 130 143 FT TURN 144 146 FT STRAND 147 152 FT HELIX 155 157 FT HELIX 160 172 FT STRAND 176 179 FT STRAND 183 186 FT HELIX 191 201 FT STRAND 205 212 FT HELIX 216 224 FT STRAND 228 233 FT HELIX 235 245 SQ SEQUENCE 248 AA; 27285 MW; 7236D2ECA2CA1951 CRC64; MIEYRIEEAV AKYREFYEFK PVRESAGIED VKSAIEHTNL KPFATPDDIK KLCLEARENR FHGVCVNPCY VKLAREELEG TDVKVVTVVG FPLGANETRT KAHEAIFAVE SGADEIDMVI NVGMLKAKEW EYVYEDIRSV VESVKGKVVK VIIETCYLDT EEKIAACVIS KLAGAHFVKT STGFGTGGAT AEDVHLMKWI VGDEMGVKAS GGIRTFEDAV KMIMYGADRI GTSSGVKIVQ GGEERYGG //