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Database: UniProt
Entry: A0A1H2RD73_9PSED
LinkDB: A0A1H2RD73_9PSED
Original site: A0A1H2RD73_9PSED 
ID   A0A1H2RD73_9PSED        Unreviewed;       258 AA.
AC   A0A1H2RD73;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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};
GN   ORFNames=SAMN05216287_0315 {ECO:0000313|EMBL:SDW17357.1};
OS   Pseudomonas kuykendallii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1007099 {ECO:0000313|EMBL:SDW17357.1, ECO:0000313|Proteomes:UP000243778};
RN   [1] {ECO:0000313|Proteomes:UP000243778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-59562 {ECO:0000313|Proteomes:UP000243778};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   EMBL; FNNU01000001; SDW17357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2RD73; -.
DR   STRING; 1007099.SAMN05216287_0315; -.
DR   OrthoDB; 6579831at2; -.
DR   Proteomes; UP000243778; Unassembled WGS sequence.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000243778}.
SQ   SEQUENCE   258 AA;  26877 MW;  54EDFDE207D53143 CRC64;
     MTDNDETLAR KVIALLDLTS LNDDDDDARI VQLCHKAMTP AGPVAAVCVF PRFVALARRS
     LDALGGHAVA VATVTNFPAG SAALDDVLAE TRQALEDGAD EIDVVYPYHA LLAGDAASGS
     ALVAACSALC EGRALLKVIL ETGELVDPLL IRRASQDAIA AGADFIKTST GKVRTNATAE
     AAEIMLACIA DSGGAVGFKP AGGMKTLPEA LVYLWLAERL NGHEWITPRH LRFGASSLLN
     DLLRRLGQAS APAMGGAY
//
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