ID   DEOC2_MESFL             Reviewed;         212 AA.
AC   Q6F0H8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Deoxyribose-phosphate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=DERA 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00114};
DE   AltName: Full=Phosphodeoxyriboaldolase 2 {ECO:0000255|HAMAP-Rule:MF_00114};
DE            Short=Deoxyriboaldolase 2 {ECO:0000255|HAMAP-Rule:MF_00114};
GN   Name=deoC2 {ECO:0000255|HAMAP-Rule:MF_00114}; OrderedLocusNames=Mfl639;
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC   Mesoplasma.
OX   NCBI_TaxID=265311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AE017263; AAT75995.1; -; Genomic_DNA.
DR   RefSeq; YP_053879.1; NC_006055.1.
DR   AlphaFoldDB; Q6F0H8; -.
DR   SMR; Q6F0H8; -.
DR   STRING; 265311.Mfl639; -.
DR   EnsemblBacteria; AAT75995; AAT75995; Mfl639.
DR   KEGG; mfl:Mfl639; -.
DR   PATRIC; fig|265311.5.peg.641; -.
DR   eggNOG; COG0274; Bacteria.
DR   HOGENOM; CLU_053595_0_2_14; -.
DR   OMA; GFKMVAI; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000006647; 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..212
FT                   /note="Deoxyribose-phosphate aldolase 2"
FT                   /id="PRO_0000231547"
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   212 AA;  23666 MW;  F5C51126138B7BB7 CRC64;
     MKLNNYIDAT LLKPDATLIE INKFVDLCII KNVRCICVHI SRIAVVKEII KNTKISISGT
     VSFPFGNATT KLKINEIKEC LKLGANEIDF VANIGNIKDH DWEKVNSEFQ KIRNSFKDII
     IKVIFETCLL TEEEIIKCCQ IAVKNKLDFV KTSTGYSKMG ATIEHVKLMK KIVNNECKVK
     ASGGIKTKNF ALELVEAGAE RIGTSSISEV LN