ID   DEOC_COREF              Reviewed;         222 AA.
AC   Q8FSJ0;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   16-JUN-2009, entry version 42.
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=CE0401;
OS   Corynebacterium efficiens.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=152794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC17211.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_737011.1; -.
DR   GeneID; 1032522; -.
DR   GenomeReviews; BA000035_GR; CE0401.
DR   KEGG; cef:CE0401; -.
DR   NMPDR; fig|196164.1.peg.401; -.
DR   HOGENOM; Q8FSJ0; -.
DR   BioCyc; CEFF196164:CE0401-MON; -.
DR   BRENDA; 4.1.2.4; 277326.
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_0000057229.
FT   ACT_SITE    156    156       Schiff-base intermediate with
FT                                acetaldehyde (By similarity).
FT   ACT_SITE    186    186       By similarity.
SQ   SEQUENCE   222 AA;  22539 MW;  E56DB37B09819089 CRC64;
     MTITRAEMAS ILDYTLLGPE VTTADLQALI DDALTLGVPT ICIPPSMMNA TKRAQDAGLR
     IATVAGFPHG KSAPLVKAAE ARLAVQYGAS EVDVVLDIAA VKAADDNALL AEMVAIREAL
     ASPVTLKFIV ESAVVDDVAL EVATHAARAA GADFIKTSTG FHPAGGATVE AVRVLAGAAQ
     GQIGVKASGG IRTWEQAVAM VEAGATRIGT SNARAILEGA PA
//