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   27-MAR-2024, entry version 121.
DE   RecName: Full=Deoxyribose-phosphate aldolase 1 {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=DERA 1 {ECO:0000255|HAMAP-Rule:MF_00114};
DE            EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase 1 {ECO:0000255|HAMAP-Rule:MF_00114};
DE   AltName: Full=Phosphodeoxyriboaldolase 1 {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=Deoxyriboaldolase 1 {ECO:0000255|HAMAP-Rule:MF_00114};
GN   Name=deoC1 {ECO:0000255|HAMAP-Rule:MF_00114}; Synonyms=dra;
GN   OrderedLocusNames=SAV0138;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   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., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC       and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00114};
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00114}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305}.
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DR   EMBL; BA000017; BAB56300.1; -; Genomic_DNA.
DR   RefSeq; WP_000667269.1; NC_002758.2.
DR   AlphaFoldDB; P61108; -.
DR   SMR; P61108; -.
DR   KEGG; sav:SAV0138; -.
DR   HOGENOM; CLU_053595_0_1_9; -.
DR   PhylomeDB; P61108; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00959; DeoC; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00114; DeoC_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR028581; DeoC_typeI.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889:SF1; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   World-2DPAGE; 0002:P61108; -.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Schiff base.
FT   CHAIN           1..220
FT                   /note="Deoxyribose-phosphate aldolase 1"
FT                   /id="PRO_0000057257"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        151
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        180
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
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
//