ID A0A1L8I769_9BACI Unreviewed; 229 AA. AC A0A1L8I769; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 13-SEP-2023, entry version 19. DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114}; DE Short=DERA {ECO:0000256|HAMAP-Rule:MF_00114}; DE EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00114}; DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114}; DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114}; DE Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114}; GN Name=deoC {ECO:0000256|HAMAP-Rule:MF_00114}; GN ORFNames=A6D91_01220 {ECO:0000313|EMBL:OJF17556.1}; OS Bacillaceae bacterium G1. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae. OX NCBI_TaxID=1836462 {ECO:0000313|EMBL:OJF17556.1, ECO:0000313|Proteomes:UP000243254}; RN [1] {ECO:0000313|EMBL:OJF17556.1, ECO:0000313|Proteomes:UP000243254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G1 {ECO:0000313|EMBL:OJF17556.1}; RA Antunes L.P., Martins L.F., Pereira R.V., Thomas A.M., Barbosa D., RA Nascimento L., Silva G.M., Condomitti G.W., Digiampietri L.A., RA Lombardi K.C., Ramos P.L., Quaggio R.B., Oliveira J.C., Pascon R.C., RA Cruz J.B., Moura L.M., Silva A.M., Setubal J.C.; RT "Microbial community structure and dynamics in thermophilic composting RT viewed through metagenomics and metatranscriptomics."; RL Submitted (AUG-2016) 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. {ECO:0000256|HAMAP-Rule:MF_00114}. 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, ECO:0000256|HAMAP- CC Rule:MF_00114}; 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. {ECO:0000256|HAMAP- CC Rule:MF_00114}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00114}. CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1 CC subfamily. {ECO:0000256|ARBA:ARBA00010936, ECO:0000256|HAMAP- CC Rule:MF_00114}. 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:OJF17556.1}. 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; LWLU01000227; OJF17556.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1L8I769; -. DR UniPathway; UPA00002; UER00468. DR Proteomes; UP000243254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule. 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 HAMAP; MF_00114; DeoC_type1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011343; DeoC. DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase. DR InterPro; IPR028581; DeoC_typeI. DR NCBIfam; TIGR00126; deoC; 1. DR PANTHER; PTHR10889:SF1; 2-DEOXY-D-RIBOSE 5-PHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR10889; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00114}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00114}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}. FT ACT_SITE 96 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114" FT ACT_SITE 162 FT /note="Schiff-base intermediate with acetaldehyde" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114" FT ACT_SITE 191 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114" SQ SEQUENCE 229 AA; 25063 MW; 69C958AD66A3DBD0 CRC64; MSEKAIAKHL HRMIDHTLLQ PAATETQIRQ LCREAEEHQF FAVCVHPHYV PLARRELQQT DVKVCTVVGF PLGLHALDVK RLEASLAVED GADELDYVIN MAHVKNGNWR GVEDEMAAMR RIKEEASRPL VIKAILETGY LTDEELVRLC QMAVACGLDF VKTSTGFGPG GATVAHVALM RQVVGDRCGV KASGGIRTKD DAVRMVQAGA NRIGTSAGLQ ILQQVNGEK //