DEOC_CAEEL
ID DEOC_CAEEL Reviewed; 303 AA.
AC Q19264;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Putative deoxyribose-phosphate aldolase;
DE Short=DERA;
DE EC=4.1.2.4;
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;
DE AltName: Full=Phosphodeoxyriboaldolase;
DE Short=Deoxyriboaldolase;
GN ORFNames=F09E5.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000250}.
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 -!- 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.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; FO081044; CCD68756.1; -; Genomic_DNA.
DR PIR; T16004; T16004.
DR RefSeq; NP_495009.1; NM_062608.5.
DR AlphaFoldDB; Q19264; -.
DR SMR; Q19264; -.
DR BioGRID; 39256; 33.
DR STRING; 6239.F09E5.3; -.
DR EPD; Q19264; -.
DR PaxDb; Q19264; -.
DR PeptideAtlas; Q19264; -.
DR EnsemblMetazoa; F09E5.3.1; F09E5.3.1; WBGene00017283.
DR GeneID; 173911; -.
DR KEGG; cel:CELE_F09E5.3; -.
DR UCSC; F09E5.3.1; c. elegans.
DR CTD; 173911; -.
DR WormBase; F09E5.3; CE02610; WBGene00017283; -.
DR eggNOG; KOG3981; Eukaryota.
DR GeneTree; ENSGT00390000007878; -.
DR HOGENOM; CLU_053595_3_0_1; -.
DR InParanoid; Q19264; -.
DR OMA; RYSGPDY; -.
DR OrthoDB; 1349979at2759; -.
DR PhylomeDB; Q19264; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-71336; Pentose phosphate pathway.
DR UniPathway; UPA00002; UER00468.
DR PRO; PR:Q19264; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017283; Expressed in larva and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IBA:GO_Central.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IBA:GO_Central.
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 InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
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 Lyase; Reference proteome; Schiff base.
FT CHAIN 1..303
FT /note="Putative deoxyribose-phosphate aldolase"
FT /id="PRO_0000057312"
FT ACT_SITE 157
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A6L0"
FT ACT_SITE 220
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000250|UniProtKB:P0A6L0"
FT ACT_SITE 256
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A6L0"
SQ SEQUENCE 303 AA; 33087 MW; 5921EA28AB7FEE0E CRC64;
MATIVPTLFS FVRDTYKGRF DVATFEREVG RDFDNQEIAQ AISKYEQEAK NLRNKDEIRK
VIQYIDLTTL NGDDTASKVV ALAKRAINPV PTDPSIHCGS VCVYPQRIAD VKKFLASSKL
NSNITSVAGG FPSGQYHLKS KVLEVELSVA DGATEIDIVI SRASALDEDW KTVHDEVLAC
KKACGSAHLK TILATGELKT LSNVYRASWA SILAGSDFIK TSTGKESVNA TLEVAYVMCT
AIKRWHELTG KKVGFKPAGG IKTVDEALSY VALVKDILGD EWLNPHLFRI GASSLLDDCL
KGL