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 27-MAR-2024, entry version 95.
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; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Entomoplasmataceae; 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 PaxDb; 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 OrthoDB; 9778711at2; -.
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; 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.
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
//
