ID   DEOC1_OCEIH             Reviewed;         221 AA.
AC   Q8EPW8;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 122.
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=OB1963;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13919.1; -; Genomic_DNA.
DR   RefSeq; WP_011066360.1; NC_004193.1.
DR   AlphaFoldDB; Q8EPW8; -.
DR   SMR; Q8EPW8; -.
DR   STRING; 221109.22777647; -.
DR   EnsemblBacteria; BAC13919; BAC13919; BAC13919.
DR   KEGG; oih:OB1963; -.
DR   eggNOG; COG0274; Bacteria.
DR   HOGENOM; CLU_053595_0_1_9; -.
DR   OMA; MNACIPP; -.
DR   OrthoDB; 1227369at2; -.
DR   PhylomeDB; Q8EPW8; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000000822; 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; -; 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   PANTHER; PTHR10889; PTHR10889; 1.
DR   PANTHER; PTHR10889:SF1; PTHR10889:SF1; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   TIGRFAMs; TIGR00126; deoC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..221
FT                   /note="Deoxyribose-phosphate aldolase 1"
FT                   /id="PRO_0000057250"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        152
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT   ACT_SITE        181
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   221 AA;  23666 MW;  81E76D434976E093 CRC64;
     MDLAKYIDHT QLKPDTTKQS IVKIVEEAKQ HEFASVCVNP HWVSYCYNEL KDTPVKVCTV
     IGFPLGATST ETKIFETNQA IADGATEVDM VINVGELKSN NDAFVEKDIR AVVEAAKGKA
     LTKVIIETSL LTEDEKVRAC KLAKNAEADY VKTSTGFSGG GATVEDIRLM RETVGPEMGV
     KASGGVRDLE QTEAMIEAGA TRIGASSGVA IVSGEQGTSD Y