ID   DEOC_ALIF1              Reviewed;         258 AA.
AC   Q5E7J7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=DERA {ECO:0000255|HAMAP-Rule:MF_00592};
DE            EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00592};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
DE            Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00592};
GN   Name=deoC {ECO:0000255|HAMAP-Rule:MF_00592}; OrderedLocusNames=VF_0504;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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_00592}.
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_00592};
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_00592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00592}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00592}.
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DR   EMBL; CP000020; AAW84999.1; -; Genomic_DNA.
DR   RefSeq; WP_005417709.1; NC_006840.2.
DR   RefSeq; YP_203887.1; NC_006840.2.
DR   AlphaFoldDB; Q5E7J7; -.
DR   SMR; Q5E7J7; -.
DR   STRING; 312309.VF_0504; -.
DR   EnsemblBacteria; AAW84999; AAW84999; VF_0504.
DR   GeneID; 64241940; -.
DR   KEGG; vfi:VF_0504; -.
DR   PATRIC; fig|312309.11.peg.495; -.
DR   eggNOG; COG0274; Bacteria.
DR   HOGENOM; CLU_053595_3_1_6; -.
DR   OMA; MNACIPP; -.
DR   OrthoDB; 1227369at2; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000000537; Chromosome I.
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_00592; DeoC_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR023649; DeoC_typeII.
DR   PANTHER; PTHR10889; PTHR10889; 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..258
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_1000072617"
FT   ACT_SITE        102
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
FT   ACT_SITE        199
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00592"
SQ   SEQUENCE   258 AA;  27724 MW;  C988C2CEB8EBFD0D CRC64;
     MSDLKAAALR ALKLMDLTTL NDNDTDEAVI ALCKNAKTAV GNTAAVCIYP RFIPIAKKTL
     REQGTPEVRI ATVTNFPHGN DDIEIAVAET KAAVAYGADE VDVVFPYRAL IAGDETTGFE
     LVKQCKEACG DVLLKVIIET GELKEEALIK KASQICIEAG ANFIKTSTGK VPVNATPEYA
     RMMLEVIRDM DVAKTVGFKP AGGVRTAEDA QAYLAMADDI LGGDWADNMH YRFGASSLLT
     NLLNTLEVTE ETADPSAY