SMART: DeoC domain annotation

DeoC DeoC/LacD family aldolase

SMART accession number:	SM01133
Description:	This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, 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:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation ((PUBMED:1655695)).
Family alignment:	View or

There are 2128 DeoC domains in 2128 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with DeoC domain is also avaliable.

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Go to specific node: Anopheles gambiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes
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
1o0y		Crystal structure of deoxyribose-phosphate aldolase (tm1559) from thermotoga maritima at 1.9 a resolution
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
1w8r		The mechanism of the schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates
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
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

Links (links to other resources describing this domain)
PFAM DeoC