ID   A0A1I7TSZ2_9PELO        Unreviewed;       303 AA.
AC   A0A1I7TSZ2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=deoxyribose-phosphate aldolase {ECO:0000256|ARBA:ARBA00012515};
DE            EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|ARBA:ARBA00031814};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g11465.t1};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g11465.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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:0000256|ARBA:ARBA00000764};
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       {ECO:0000256|ARBA:ARBA00004816}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC       subfamily. {ECO:0000256|ARBA:ARBA00009473}.
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DR   AlphaFoldDB; A0A1I7TSZ2; -.
DR   STRING; 1561998.A0A1I7TSZ2; -.
DR   WBParaSite; Csp11.Scaffold629.g11465.t1; Csp11.Scaffold629.g11465.t1; Csp11.Scaffold629.g11465.
DR   eggNOG; KOG3981; Eukaryota.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
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   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889:SF3; 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   Schiff base {ECO:0000256|PIRSR:PIRSR001357-50}.
FT   ACT_SITE        220
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
FT   ACT_SITE        256
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
SQ   SEQUENCE   303 AA;  33124 MW;  3F385CB1A191349E CRC64;
     MATIVPTLFS LVRDSRRGVF DAATFEREVA RDFDNQEITQ AINRYEQEGK SMRNKEEIRK
     VIQYIDLTTL NGDDTASKVV ALAKRAINPI PTDPSIHCGS VCVYPQRIAD VKKFLNATKQ
     NCHITGVAGG FPSGQYHLQS KVLECELSVA DGATEIDIVI SRASALEEDW KTVHDEVQAC
     KNACGSAHLK TILATGELKT LSNVYKASWA SILAGSDFIK TSTGKESVNA TLEVAYVMCS
     AVKRWYELTG KKVGFKPAGG IKTVDEALSY VALVKDILGE QWLNPTLFRI GASSLLDDCL
     KAL
//