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InterPro: IPR011343 Deoxyribose-phosphate aldolase

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1511 proteins

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Matches in BioMart

Accession

IPR011343 DeoC

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF001357	DeoC	1404
PANTHER	PTHR10889	DeoC	1499
TIGRFAMs	TIGR00126	deoC	1440
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002915 Deoxyribose-phosphate aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase

Contains

IPR013785 Aldolase-type TIM barrel

GO Term annotation Help

Process

GO:0009264 deoxyribonucleotide catabolic process

Function

GO:0004139 deoxyribose-phosphate aldolase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

Class I aldolases catalyse carbon-carbon bond formation using a 'Schiff base' mechanism. This entry represents deoxyribose-phosphate aldolase, a widely distributed enzyme, which catalyses the following reversible reaction:

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde

While the physiological role of this enzyme remains unknown in eukaryotes, in prokaroytes it is thought to function in the catabolism of deoxyribonucleotides [1, 2].

In all studied structures, the deoxyribose-phophate aldolase subunits adopt the classical eight-bladed TIM barrel fold [3, 4, 5]. The oligomerisation state of the enzyme appears to depend on the living temperature of the organism - the Escherichia coli enzyme (P0A6L0) is a homodimer, while the enzymes from the thermophilic microorganisms Thermus thermophilus and Aeropyrum pernix (Q9Y948) are homotetramers. The degree of oligomerisation does not, however, appear to affect catalysis.

Structural links Help

PDB - click here

SCOP: c.1.10.1

CATH: 3.20.20.70

Database links Help

Enzyme: EC:4.1.2.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011343

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O66540 Deoxyribose-phosphate aldolase

P73618 Deoxyribose-phosphate aldolase

Q19264 Putative deoxyribose-phosphate aldolase

Q91YP3 Putative deoxyribose-phosphate aldolase

Q9Y315 Putative deoxyribose-phosphate aldolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002915	Deoxyribose-phosphate aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase
IPR013785	Aldolase-type TIM barrel
IPR011343	Deoxyribose-phosphate aldolase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Sgarrella F, Del Corso A, Tozzi MG, Camici M. Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties. Biochim. Biophys. Acta 1118 130-3 1992 [PubMed: 1730028] http://dx.doi.org/10.1016/0167-4838(92)90139-5
2.	Munch-Petersen A. Deoxyribonucleoside catabolism and thymine incorporation in mutants of Escherichia coli lacking deoxyriboaldolase. Eur. J. Biochem. 15 191-202 1970 [PubMed: 4923156] http://dx.doi.org/10.1111/j.1432-1033.1970.tb00994.x
3.	Lokanath NK, Shiromizu I, Ohshima N, Nodake Y, Sugahara M, Yokoyama S, Kuramitsu S, Miyano M, Kunishima N. Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability. Acta Crystallogr. D Biol. Crystallogr. 60 1816-23 2004 [PubMed: 15388928] http://dx.doi.org/10.1107/S0907444904020190
4.	Heine A, DeSantis G, Luz JG, Mitchell M, Wong CH, Wilson IA. Observation of covalent intermediates in an enzyme mechanism at atomic resolution. Science 294 369-74 2001 [PubMed: 11598300] http://dx.doi.org/10.1126/science.1063601
5.	Sakuraba H, Tsuge H, Shimoya I, Kawakami R, Goda S, Kawarabayasi Y, Katunuma N, Ago H, Miyano M, Ohshima T. The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-d-ribose-5-phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix. J. Biol. Chem. 278 10799-806 2003 [PubMed: 12529358] http://dx.doi.org/10.1074/jbc.M212449200

Additional Reading Open in usermanual
	Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 151 2007 100-10 [PubMed: 17125854] http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
	Heine A, Luz JG, Wong CH, Wilson IA. Analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99A resolution. J. Mol. Biol. 343 2004 1019-34 [PubMed: 15476818] http://dx.doi.org/10.1016/j.jmb.2004.08.066
	Sakuraba H, Yoneda K, Yoshihara K, Satoh K, Kawakami R, Uto Y, Tsuge H, Takahashi K, Hori H, Ohshima T. Sequential aldol condensation catalyzed by hyperthermophilic 2-deoxy-d-ribose-5-phosphate aldolase. Appl. Environ. Microbiol. 73 2007 7427-34 [PubMed: 17905878] http://dx.doi.org/10.1128/AEM.01101-07

InterPro 23.1