DEOC_STREM
ID DEOC_STREM Reviewed; 220 AA.
AC B4U2S5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=DERA {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 {ECO:0000255|HAMAP-Rule:MF_00114};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
GN Name=deoC {ECO:0000255|HAMAP-Rule:MF_00114}; OrderedLocusNames=Sez_0934;
OS Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=552526;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGCS10565;
RX PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA Musser J.M.;
RT "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT causing epidemic nephritis: new information about an old disease.";
RL PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG62292.1; -; Genomic_DNA.
DR RefSeq; WP_012515563.1; NC_011134.1.
DR AlphaFoldDB; B4U2S5; -.
DR SMR; B4U2S5; -.
DR EnsemblBacteria; ACG62292; ACG62292; Sez_0934.
DR GeneID; 64011144; -.
DR KEGG; sez:Sez_0934; -.
DR HOGENOM; CLU_053595_0_2_9; -.
DR OMA; MNACIPP; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000001873; 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..220
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_1000094855"
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 220 AA; 22976 MW; 78F993F479A3585B CRC64;
MNINKYIDHT LLKADSVQSQ LDQLIEEAKA YDFASVCVNP CWVAYAAKAL KGTDVKVCTV
VGFPLGATTS ATKAFETKDA IENGADEIDM VINIGLLKQG DYQAVEDDMR AVVEASGDKL
VKVIIEACLL TDDEKVKACQ LAVNAGVDFV KTSTGFSTGG ATVSDVKLMR QTVGPDIGVK
AAGGARSLED ALAFVEAGAT RIGTSAGVTI MKGEVANGGY
