ID   DEOC1_STAAR             Reviewed;         220 AA.
AC   Q6GKG7;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Deoxyribose-phosphate aldolase 1;
DE            EC=4.1.2.4;
DE   AltName: Full=Phosphodeoxyriboaldolase 1;
DE            Short=Deoxyriboaldolase 1;
DE            Short=DERA 1;
GN   Name=deoC1; Synonyms=dra; OrderedLocusNames=SAR0140;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39167.1; -; Genomic_DNA.
DR   RefSeq; YP_039605.1; -.
DR   GeneID; 2859268; -.
DR   GenomeReviews; BX571856_GR; SAR0140.
DR   KEGG; sar:SAR0140; -.
DR   HOGENOM; Q6GKG7; -.
DR   OMA; Q6GKG7; FPSGKHH.
DR   BioCyc; SAUR282458:SAR0140-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    220       Deoxyribose-phosphate aldolase 1.
FT                                /FTId=PRO_0000057261.
FT   ACT_SITE    151    151       Schiff-base intermediate with
FT                                acetaldehyde (By similarity).
FT   ACT_SITE    180    180       By similarity.
SQ   SEQUENCE   220 AA;  23501 MW;  51D7A826E8BCF6AB CRC64;
     MKFEKYIDHT LLKPESTRTQ IDQIIDEAKA YNFKSVCVNP THVKYAAERL ADSEVLVCTV
     IGFPLGASTT ATKVFETEDA IQNGADEIDM VINIGALKDG RFDDVQQDIE AVVKAAEGHT
     VKVIIETVLL DHDEIVKASE LTKAAGADFV KTSTGFAGGG ATAEDVKLMK DTVGADVEVK
     ASGGVRNLED FNKMVEAGAT RIGASAGVQI MQGLEADSDY
//