ID   DEOC_BOVIN              Reviewed;         318 AA.
AC   Q3T0V9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Deoxyribose-phosphate aldolase;
DE            Short=DERA;
DE            EC=4.1.2.4 {ECO:0000250|UniProtKB:Q9Y315};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;
DE   AltName: Full=Phosphodeoxyriboaldolase;
DE            Short=Deoxyriboaldolase;
GN   Name=DERA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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. Participates in stress granule (SG) assembly. May allow ATP
CC       production from extracellular deoxyinosine in conditions of energy
CC       deprivation. {ECO:0000250|UniProtKB:Q9Y315}.
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:0000250|UniProtKB:Q9Y315};
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   -!- SUBUNIT: Interacts with YBX1. {ECO:0000250|UniProtKB:Q9Y315}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y315}.
CC       Cytoplasmic granule {ECO:0000250|UniProtKB:Q9Y315}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9Y315}. Note=Recruited to stress granules but
CC       not to processing bodies upon arsenite or clotrimazole treatment or
CC       energy deprivation. {ECO:0000250|UniProtKB:Q9Y315}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC102242; AAI02243.1; -; mRNA.
DR   RefSeq; NP_001069496.1; NM_001076028.2.
DR   AlphaFoldDB; Q3T0V9; -.
DR   SMR; Q3T0V9; -.
DR   STRING; 9913.ENSBTAP00000007367; -.
DR   PaxDb; Q3T0V9; -.
DR   PeptideAtlas; Q3T0V9; -.
DR   PRIDE; Q3T0V9; -.
DR   Ensembl; ENSBTAT00000007367; ENSBTAP00000007367; ENSBTAG00000022167.
DR   GeneID; 534558; -.
DR   KEGG; bta:534558; -.
DR   CTD; 51071; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022167; -.
DR   VGNC; VGNC:28009; DERA.
DR   eggNOG; KOG3981; Eukaryota.
DR   GeneTree; ENSGT00390000007878; -.
DR   HOGENOM; CLU_053595_3_0_1; -.
DR   InParanoid; Q3T0V9; -.
DR   OMA; RYSGPDY; -.
DR   OrthoDB; 1349979at2759; -.
DR   TreeFam; TF314251; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000022167; Expressed in liver and 106 other tissues.
DR   ExpressionAtlas; Q3T0V9; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0046121; P:deoxyribonucleoside catabolic process; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Nucleus; Reference proteome; Schiff base.
FT   CHAIN           1..318
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_0000283798"
FT   ACT_SITE        155
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L0"
FT   ACT_SITE        218
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y315"
FT   ACT_SITE        254
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y315"
SQ   SEQUENCE   318 AA;  35246 MW;  DE1545BD35BCB714 CRC64;
     MSAHQQGTEL DLSWISKIQV NKPAVLRRAE QIQARRPVKK EWQAAWLLKA VTCIDLTTLS
     GDDTASNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPARVCDAV RALKAAGCDI
     PVASVATGFP AAQTHLKTRL EEIRLAVEDG ATEIDVVINR TLVLTGQWKA LYDEIRQFRK
     ACGEAHLKTI LATGELGSLT NVYKASMIAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI
     RDFFWKTGNK VGFKPAGGIR SAKDSLVWLS LIKEELGDEW MKPELFRIGA STLLADIERQ
     IYHHVTGRYA AYHDLPMS