ID   DEOC_BACHK              Reviewed;         223 AA.
AC   Q6HK62;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=BT9727_1732;
OS   Bacillus thuringiensis subsp. konkukian.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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.
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DR   EMBL; AE017355; AAT63350.1; -; Genomic_DNA.
DR   RefSeq; YP_036064.1; -.
DR   GeneID; 2856540; -.
DR   GenomeReviews; AE017355_GR; BT9727_1732.
DR   KEGG; btk:BT9727_1732; -.
DR   HOGENOM; Q6HK62; -.
DR   OMA; Q6HK62; AKMIDHT.
DR   BioCyc; BTHU281309:BT9727_1732-MON; -.
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    223       Deoxyribose-phosphate aldolase.
FT                                /FTId=PRO_0000231533.
FT   ACT_SITE    152    152       Schiff-base intermediate with
FT                                acetaldehyde (By similarity).
FT   ACT_SITE    181    181       By similarity.
SQ   SEQUENCE   223 AA;  23411 MW;  2A98ABB54B10BA39 CRC64;
     MNIAKLIDHT ILKANTTKED VMKVIEEAKE YKFASVCINP TWVKLAAEEL AGHDVDVCTV
     IGFPLGASTT ETKAFETKDA IAKGATEVDM VINVGALKDG DNELVEKDIY EVVQAAKGKA
     LVKVIIETCL LTDEEKVRAC ELSVKAGADF VKTSTGFSTG GATAEDIALM RKTVGPNVGV
     KASGGVRTRE DAEKMVAAGA SRVGASASVA IVLNDAKGAT DNY
//