ID DEOC_MYCA1 Reviewed; 223 AA. AC A0QLL2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114}; DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114}; DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114}; DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114}; DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114}; DE Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114}; GN Name=deoC {ECO:0000255|HAMAP-Rule:MF_00114}; GN OrderedLocusNames=MAV_4672; OS Mycobacterium avium (strain 104). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=243243; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=104; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) 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:0000255|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:0000255|HAMAP-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:0000255|HAMAP- CC Rule:MF_00114}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00114}. CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1 CC subfamily. {ECO:0000255|HAMAP-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; CP000479; ABK67136.1; -; Genomic_DNA. DR RefSeq; WP_011726185.1; NC_008595.1. DR PDB; 3NG3; X-ray; 2.15 A; A/B/C/D=1-223. DR PDBsum; 3NG3; -. DR AlphaFoldDB; A0QLL2; -. DR SMR; A0QLL2; -. DR KEGG; mav:MAV_4672; -. DR HOGENOM; CLU_053595_0_0_11; -. DR UniPathway; UPA00002; UER00468. DR EvolutionaryTrace; A0QLL2; -. DR Proteomes; UP000001574; 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: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; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Lyase; Schiff base. FT CHAIN 1..223 FT /note="Deoxyribose-phosphate aldolase" FT /id="PRO_1000015324" FT ACT_SITE 92 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114" FT ACT_SITE 158 FT /note="Schiff-base intermediate with acetaldehyde" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114" FT ACT_SITE 188 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114" FT HELIX 5..9 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 12..15 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 23..36 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 48..53 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:3NG3" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 73..85 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 97..101 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 105..119 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 139..151 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 171..181 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 184..192 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 196..204 FT /evidence="ECO:0007829|PDB:3NG3" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:3NG3" FT HELIX 215..220 FT /evidence="ECO:0007829|PDB:3NG3" SQ SEQUENCE 223 AA; 21723 MW; 33A436559EB7FC1A CRC64; MTPTRAQLAA FVDHTLLKPE ATAADVAALV TEAAELGVYA VCVSPPMVPA AVQAGAGVRV ASVAGFPSGK HVSAVKAHEA ALAVASGAAE IDMVIDVGAA LAGDLDGVRA DIAAVRGAVG GAVLKVIVES SALLALADEH TLVRVCRAAE DAGADFVKTS TGFHPSGGAS VRAVALMAEA VGGRLGVKAS GGIRTAADAL AMLDAGATRL GLSGTRAVLD GLG //