ID   DEOC_CORDI              Reviewed;         218 AA.
AC   Q6NJX0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
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=DIP0273;
OS   Corynebacterium diphtheriae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   MEDLINE=22965443; PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L.,
RA   Whitehead S., Barrell B.G., Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium
RT   diphtheriae NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(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; BX248354; CAE48777.1; -; Genomic_DNA.
DR   RefSeq; NP_938661.1; -.
DR   GeneID; 2648850; -.
DR   GenomeReviews; BX248353_GR; DIP0273.
DR   KEGG; cdi:DIP0273; -.
DR   NMPDR; fig|257309.1.peg.252; -.
DR   HOGENOM; Q6NJX0; -.
DR   OMA; Q6NJX0; FPSGKHH.
DR   BioCyc; CDIP257309:DIP0273-MON; -.
DR   BRENDA; 4.1.2.4; 20483.
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    218       Deoxyribose-phosphate aldolase.
FT                                /FTId=PRO_0000231537.
FT   ACT_SITE    152    152       Schiff-base intermediate with
FT                                acetaldehyde (By similarity).
FT   ACT_SITE    182    182       By similarity.
SQ   SEQUENCE   218 AA;  22352 MW;  A6BB20B99D4159AE CRC64;
     MTTRNDVAQM IDHTLLKPEA TTDDFKALIA DAVRLGTYSV CVSPSALPVE VPENLHVATV
     VGFPSGAVKP EIKAAEAART VADGAEEVDM VINIALAKEG KFDELEAEIK AVRDAVPAPG
     ILKVILETAA LTDDEIVAAC KASENAGADF VKTSTGFHPA GGASVHAVEI MHATVGGRLG
     IKASGGIRTA KDALAMIEAG ATRLGLSASA AILEELGE
//