ID   DEOC1_STAAM             Reviewed;         220 AA.
AC   P61108; Q99X77;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   03-NOV-2009, entry version 42.
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=SAV0138;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21311952; PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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-alpha-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; BA000017; BAB56300.1; -; Genomic_DNA.
DR   RefSeq; NP_370662.1; -.
DR   HSSP; Q9X1P5; 1O0Y.
DR   STRING; P61108; -.
DR   World-2DPAGE; 0002:P61108; -.
DR   GeneID; 1120097; -.
DR   GenomeReviews; BA000017_GR; SAV0138.
DR   KEGG; sav:SAV0138; -.
DR   HOGENOM; P61108; -.
DR   OMA; AKMIDHT; -.
DR   BioCyc; SAUR158878:SAV0138-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   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Lyase; Schiff base.
FT   CHAIN         1    220       Deoxyribose-phosphate aldolase 1.
FT                                /FTId=PRO_0000057257.
FT   ACT_SITE    151    151       Schiff-base intermediate with
FT                                acetaldehyde (By similarity).
FT   ACT_SITE    180    180       By similarity.
SQ   SEQUENCE   220 AA;  23472 MW;  A77DAC561C6B70A3 CRC64;
     MKFEKYIDHT LLKPESTRTQ IDQIIDEAKA YNFKSVCVNP THVKYAAERL ADSEVLVCTV
     IGFPLGASTT ATKAFETEDA IQNGADEIDM VINIGALKDG RFDDVQQDIE AVVKAAKGHT
     VKVIIETVLL DHDEIVKASE LTKAAGADFV KTSTGFAGGG ATAEDVKLMK DTVGADVEVK
     ASGGVRNLED FNKMVEAGAT RIGASAGVQI MQGLEADSDY
//