ID A3DFT0_ACET2 Unreviewed; 222 AA. AC A3DFT0; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 10-JUN-2026, entry version 124. 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 OrderedLocusNames=Cthe_1583 {ECO:0000313|EMBL:ABN52809.1}; OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales; OC Acetivibrionaceae; Acetivibrio. OX NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN52809.1, ECO:0000313|Proteomes:UP000002145}; RN [1] {ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., RA Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABN52809.1, ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RX PubMed=24295562; DOI=10.1186/1754-6834-6-179; RA Wilson C.M., Rodriguez M.Jr., Johnson C.M., Martin S.L., Chu T.M., RA Wolfinger R.D., Hauser L.J., Land M.L., Klingeman D.M., Syed M.H., RA Ragauskas A.J., Tschaplinski T.J., Mielenz J.R., Brown S.D.; RT "Global transcriptome analysis of Clostridium thermocellum ATCC 27405 RT during growth on dilute acid pretreated Populus and switchgrass."; RL Biotechnol. Biofuels 6:179-179(2013). 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|ARBA:ARBA00056337, ECO:0000256|HAMAP- CC Rule:MF_00114}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + CC acetaldehyde; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343, CC ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00048791, 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 --------------------------------------------------------------------------- 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; CP000568; ABN52809.1; -; Genomic_DNA. DR RefSeq; WP_003517326.1; NC_009012.1. DR AlphaFoldDB; A3DFT0; -. DR STRING; 203119.Cthe_1583; -. DR GeneID; 35804502; -. DR KEGG; cth:Cthe_1583; -. DR eggNOG; COG0274; Bacteria. DR HOGENOM; CLU_053595_0_2_9; -. DR OrthoDB; 9778711at2; -. DR UniPathway; UPA00002; UER00468. DR Proteomes; UP000002145; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006018; P:2-deoxyribose 1-phosphate catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:TreeGrafter. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00959; DeoC; 1. DR FunFam; 3.20.20.70:FF:000044; Deoxyribose-phosphate aldolase; 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; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR10889:SF1; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00114}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00114}; KW Reference proteome {ECO:0000313|Proteomes:UP000002145}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_00114}. FT ACT_SITE 91 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114" FT ACT_SITE 153 FT /note="Schiff-base intermediate with acetaldehyde" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114" FT ACT_SITE 182 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114" SQ SEQUENCE 222 AA; 24401 MW; 52AC677B3B75A3C9 CRC64; MNTQDILSHV DHTLLLQTAT WPEIQALCDD AIKYQTASVC IPPCYVARAK EYVGDRMVIC TVIGFPNGNM TTAAKVFETQ DAIANGADEI DMVINIGALK NKEYDYVLKE IKAIKQACGE RILKVIIETC LLTEEEKIVM CDLVTRSGAD YIKTSTGFST AGATFEDIEL FAKHVGPNVK IKAAGGISNF NDARKYIELG ADRLGTSRLV KLMKSQSYDG LY //