ID   DEOC_ECOK1              Reviewed;         259 AA.
AC   A1AJU8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Ecok1_44440; ORFNames=APECO1_2000;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(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 2
CC       subfamily.
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DR   EMBL; CP000468; ABJ03938.1; -; Genomic_DNA.
DR   RefSeq; YP_860062.1; -.
DR   SMR; A1AJU8; 1-251.
DR   GeneID; 4491976; -.
DR   GenomeReviews; CP000468_GR; Ecok1_44440.
DR   KEGG; ecv:APECO1_2000; -.
DR   OMA; A1AJU8; CKEACGD.
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_00592; -; 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   Acetylation; Complete proteome; Cytoplasm; Lyase; Schiff base.
FT   CHAIN         1    259       Deoxyribose-phosphate aldolase.
FT                                /FTId=PRO_1000072596.
FT   ACT_SITE    167    167       Schiff-base intermediate with
FT                                acetaldehyde (By similarity).
FT   ACT_SITE    201    201       By similarity.
FT   MOD_RES     167    167       N6-acetyllysine (By similarity).
SQ   SEQUENCE   259 AA;  27760 MW;  3D6F46383DE40F52 CRC64;
     MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL
     KEQGTPEIRI ATVTNFPHGN DDIEIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD
     LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE
     SARIMMEVIR DMGVEKIVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL
     LASLLKALGH GDGKSASSY
//