DEOC2_CUTAK
ID DEOC2_CUTAK Reviewed; 224 AA.
AC Q6A655;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=PPA2045;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT83758.1; -; Genomic_DNA.
DR RefSeq; WP_002516188.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A655; -.
DR SMR; Q6A655; -.
DR STRING; 267747.PPA2045; -.
DR EnsemblBacteria; AAT83758; AAT83758; PPA2045.
DR GeneID; 66621949; -.
DR KEGG; pac:PPA2045; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_0_0_11; -.
DR OMA; KRGIGNE; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000000603; 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; Schiff base.
FT CHAIN 1..224
FT /note="Deoxyribose-phosphate aldolase 2"
FT /id="PRO_0000231560"
FT ACT_SITE 94
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 157
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 187
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
SQ SEQUENCE 224 AA; 23009 MW; C26A671745B96D6B CRC64;
MSSAPLSATE LAGMIDHTLL TPEATHNDVA KLVADAKKYG TWSVCVSPSM LPLNLDMGDV
HLAVVCGFPS GKHTSAVKAA EAREAIAAGA EEVDMVINLG LVKEGRWEDV TADIAAVKQA
VPDPKILKVI IESAVLTDDE IVRACQAAEK AGADFVKTST GFHPRGGASV EAVKVMADTV
GGRLGVKASG GIRDYQTACA MVEAGATRLG VSSTAKILAG APTE