ID   DEOC_BACHD              Reviewed;         224 AA.
AC   Q9KD67;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 57.
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; Synonyms=dra; OrderedLocusNames=BH1352;
OS   Bacillus halodurans.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
RX   MEDLINE=20512582; PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05071.1; -; Genomic_DNA.
DR   PIR; H83818; H83818.
DR   RefSeq; NP_242218.1; -.
DR   HSSP; Q9X1P5; 1O0Y.
DR   GeneID; 892275; -.
DR   GenomeReviews; BA000004_GR; BH1352.
DR   KEGG; bha:BH1352; -.
DR   NMPDR; fig|272558.1.peg.1352; -.
DR   HOGENOM; Q9KD67; -.
DR   OMA; Q9KD67; AKMIDHT.
DR   BioCyc; BHAL272558:BH1352-MON; -.
DR   BRENDA; 4.1.2.4; 191865.
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    224       Deoxyribose-phosphate aldolase.
FT                                /FTId=PRO_0000057223.
FT   ACT_SITE    155    155       Schiff-base intermediate with
FT                                acetaldehyde (By similarity).
FT   ACT_SITE    184    184       By similarity.
SQ   SEQUENCE   224 AA;  23362 MW;  5CC79183BB424502 CRC64;
     MSRSIAQMID HTLLKPNTTE DQIVKLCEEA KEYSFASVCV NPTWVALAAQ LLKDAPDVKV
     CTVIGFPLGA TTPEVKAFET TNAIENGATE VDMVINIGAL KDKQYELVGR DIQAVVKAAE
     GKALTKVIIE TSLLTEEEKK AACELAVKAG ADFVKTSTGF SGGGATAEDI ALMRKVVGPN
     LGVKASGGVR DLSDAKAMID AGATRIGASA GVAIVNGERS EGSY
//