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Database: UniProt
Entry: A0A1I6PMF8_9PSEU
LinkDB: A0A1I6PMF8_9PSEU
Original site: A0A1I6PMF8_9PSEU 
ID   A0A1I6PMF8_9PSEU        Unreviewed;       288 AA.
AC   A0A1I6PMF8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05660874_00933 {ECO:0000313|EMBL:SFS41374.1};
OS   Saccharopolyspora flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=95161 {ECO:0000313|EMBL:SFS41374.1, ECO:0000313|Proteomes:UP000198852};
RN   [1] {ECO:0000313|EMBL:SFS41374.1, ECO:0000313|Proteomes:UP000198852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44771 {ECO:0000313|EMBL:SFS41374.1,
RC   ECO:0000313|Proteomes:UP000198852};
RA   de Groot N.N.;
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; FOZX01000001; SFS41374.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6PMF8; -.
DR   STRING; 95161.SAMN05660874_00933; -.
DR   Proteomes; UP000198852; 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;
SQ   SEQUENCE   288 AA;  30460 MW;  342248B1660813EF CRC64;
     MDQVGLEQRA AGLGTRSVKK DSKLRAIDIA ISMVDLTTLE GADTEGKVRS LCAKARRPDP
     GWDGVPPVAA VCVYSDLAAT AVAELGGSGV RVASVATAFP SGRAARAVKL ADVEHAVAAG
     ADEIDMVIDR GAFLAGRYGQ VFDEIQAVKE ACGDAHLKVI LETGELATYD NVRRASWLAL
     LAGGDFIKTS TGKVSPAATL PVTHLMLQAV RDWRDATGEL RGVKPAGGIR STKDAIRYLV
     AVNEVAGPEW LTPELFRFGA SSLLNDLLMQ RRTQLDGHYS GPEHVAVD
//
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