ID A0A3B9LI15_9BACT Unreviewed; 112 AA. AC A0A3B9LI15; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 24-JUL-2024, entry version 11. 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 Flags: Fragment; GN ORFNames=DCG89_09645 {ECO:0000313|EMBL:HAF04046.1}; OS Spartobacteria bacterium. OC Bacteria; Verrucomicrobiota; Spartobacteria. OX NCBI_TaxID=2052183 {ECO:0000313|EMBL:HAF04046.1, ECO:0000313|Proteomes:UP000259422}; RN [1] {ECO:0000313|EMBL:HAF04046.1, ECO:0000313|Proteomes:UP000259422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA10877 {ECO:0000313|EMBL:HAF04046.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HAF04046.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DMCG01000228; HAF04046.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3B9LI15; -. DR Proteomes; UP000259422; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:InterPro. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:TreeGrafter. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011343; DeoC. DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1. DR SUPFAM; SSF51569; Aldolase; 1. PE 4: Predicted; FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:HAF04046.1" SQ SEQUENCE 112 AA; 12332 MW; AD0ED0EE1A3337BA CRC64; EIAMRAGVDF IKTSTGKISP AATMPVTLVM LEAIRDYFYE TGIRIGMKPA GGIRTAKQAL AWLVMLKETL GDDWLTPDLF RFGASTLVND VLMQIVKTVD GNYQGPDYFS LP //