DeoCDeoC/LacD family aldolase
|SMART accession number:||SM01133|
|Description:||This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:184.108.40.206, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Q57843 and P76143. The family also includes tagatose 1,6-diphosphate aldolase ( EC:220.127.116.11) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation ((PUBMED:1655695)).|
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- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing DeoC domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with DeoC domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing DeoC domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
Cellular role: metabolism
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Sgarrella F, Del Corso A, Tozzi MG, Camici M
- Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties.
- Biochim Biophys Acta. 1992; 1118: 130-3
- Display abstract
Deoxyribose 5-phosphate aldolase was purified 41 times from Bacillus cereusinduced by growth on deoxyribonucleosides. The purification procedure includesammonium sulphate fractionation, gel filtration on Sephadex G-100, ion-exchangechromatography on DEAE-Sephacel and preparative electrophoresis on 10%polyacrylamide gel. The enzyme is stable above pH 6.5, but is rapidly inactivatedby sulfhydryl reagents. Being insensitive to EDTA, it may be considered as aClass I aldolase. Among a number of compounds tested (including some carboxylicacids, free and phosphorylated pentoses, nucleotides and nucleosides), none hasbeen found to affect the enzyme activity. The enzyme appears to be dimeric, with a subunit Mr of 23,600. A Km of 4.4 x 10(-4) M was calculated for dRib 5-P.
- Rosey EL, Oskouian B, Stewart GC
- Lactose metabolism by Staphylococcus aureus: characterization of lacABCD, thestructural genes of the tagatose 6-phosphate pathway.
- J Bacteriol. 1991; 173: 5992-8
- Display abstract
The nucleotide and deduced amino acid sequences of the lacA and lacB genes of theStaphylococcus aureus lactose operon (lacABCDFEG) are presented. The primarytranslation products are polypeptides of 142 (Mr = 15,425) and 171 (Mr = 18,953) amino acids, respectively. The lacABCD loci were shown to encode enzymes of thetagatose 6-phosphate pathway through both in vitro studies and complementationanalysis in Escherichia coli. A serum aldolase assay, modified to allow detectionof the tagatose 6-phosphate pathway enzymes utilizing galactose 6-phosphate orfructose phosphate analogs as substrate, is described. Expression of both lacAand lacB was required for galactose 6-phosphate isomerase activity. LacC (34 kDa)demonstrated tagatose 6-phosphate kinase activity and was found to sharesignificant homology with LacC from Lactococcus lactis and with both the minor6-phosphofructokinase (PfkB) and 1-phosphofructokinase (FruK) from E. coli.Detection of tagatose 1,6-bisphosphate aldolase activity was dependent onexpression of the 36-kDa protein specified by lacD. The LacD protein is highlyhomologous with LacD of L. lactis. Thus, the lacABCD genes comprise the tagatose 6-phosphate pathway and are cotranscribed with genes lacFEG, which specifyproteins for transport and cleavage of lactose in S. aureus.
- Structure (3D structures containing this domain)
3D Structures of DeoC domains in PDB
PDB code Main view Title 1j2w Tetrameric Structure of aldolase from Thermus thermophilus HB8 1jcj OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION 1jcl OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION 1ktn Structural Genomics, Protein EC1535 1mzh QR15, an Aldolase 1n7k Unique tetrameric structure of deoxyribose phosphate aldolase from Aeropyrum pernix 1ojx Crystal structure of an Archaeal fructose 1,6-bisphosphate aldolase 1ok4 Archaeal fructose 1,6-bisphosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate 1ok6 Orthorhombic crystal form of an Archaeal fructose 1,6-bisphosphate aldolase 1p1x Comparison of class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase determined at 0.99 Angstrom resolution 1to3 Structure of yiht from Salmonella typhimurium 1ub3 Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8 1vcv Structure of 2-deoxyribose-5-phosphate aldolase from Pyrobaculum aerophilum 1w8s The mechanism of the Schiff Base Forming Fructose-1,6-bisphosphate Aldolase: Structural analysis of reaction intermediates. 2a4a Deoxyribose-phosphate aldolase from P. yoelii 2qjg M. jannaschii ADH synthase complexed with F1,6P 2qjh M. jannaschii ADH synthase covalently bound to dihydroxyacetone phosphate 2qji M. jannaschii ADH synthase complexed with dihydroxyacetone phosphate and glycerol 2yce Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate. 3gkf Crystal Structure of E. coli LsrF 3glc Crystal Structure of E. coli LsrF in complex with Ribose-5-phosphate 3gnd Crystal Structure of E. coli LsrF in complex with Ribulose-5-phosphate 3iv3 The Structure of a putative tagatose 1,6-aldolase from Streptococcus mutans 3jrk A putative tagatose 1,6-diphosphate aldolase from Streptococcus pyogenes 3kao Crystal structure of tagatose 1,6-diphosphate aldolase from Staphylococcus aureus 3mhf Tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes 3mhg Dihydroxyacetone phosphate carbanion intermediate in tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes 3myo Crystal structure of tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes 3myp Crystal structure of tagatose-1,6-bisphosphate aldolase from Staphylococcus aureus 3ndo Crystal structure of deoxyribose phosphate aldolase from mycobacterium smegmatis 3ng3 Crystal structure of deoxyribose phosphate aldolase from mycobacterium avium 104 in a schiff base with an unknown aldehyde 3ngj Crystal structure of a putative deoxyribose-phosphate aldolase from Entamoeba histolytica 3npu Optimization of the in silico designed Kemp eliminase KE70 by computational design and directed evolution 3npv Optimization of the in silico designed Kemp eliminase KE70 by computational design and directed evolution 3npw In silico designed of an improved Kemp eliminase KE70 mutant by computational design and directed evolution 3npx Optimization of the in silico designed Kemp eliminase KE70 by computational design and directed evolution 3nq2 Optimization of the in silico designed Kemp eliminase KE70 by computational design and directed evolution R2 3/5G 3nq8 Optimization of the in silico designed Kemp eliminase KE70 by computational design and directed evolution R4 8/5A 3nqv Optimization of the in silico designed Kemp eliminase KE70 by computational design and directed evolution R5 7/4A 3nr0 Optimization of the in silico designed Kemp eliminase KE70 by computational design and directed evolution R6 6/10A 3oa3 Crystal structure of a putative deoxyribose-phosphate aldolase from Coccidioides immitis 3q2d 3qyq 1.8 Angstrom resolution crystal structure of a putative deoxyribose-phosphate aldolase from Toxoplasma gondii ME49 3r12 Crystal structure of a Deoxyribose-phosphate aldolase (TM_1559) from THERMOTOGA MARITIMA at 1.75 A resolution 3r13 Crystal structure of a Deoxyribose-phosphate aldolase (TM_1559) from THERMOTOGA MARITIMA at 1.83 A resolution 4eiv 1.37 Angstrom resolution crystal structure of apo-form of a putative deoxyribose-phosphate aldolase from Toxoplasma gondii ME49 4moz Fructose-bisphosphate aldolase from Slackia heliotrinireducens DSM 20476
- Links (links to other resources describing this domain)