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

Protein matches Help

UniProtKB

Matches:

2790 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR002915 DeoC/AroFGH_arch

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01791	DeoC	2790
Signatures in BioMart

InterPro Relationships Help

Children

IPR005927 Tagatose 1,6-diphosphate aldolase, Gram-positive
IPR010210 Predicted phospho-2-dehydro-3-deoxyheptonate aldolase
IPR011343 Deoxyribose-phosphate aldolase
IPR017291 Aldolase, YihT

Contains

IPR013785 Aldolase-type TIM barrel

GO Term annotation Help

Function

GO:0016829 lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

This family includes the enzyme deoxyribose-phosphate aldolase, which is involved in nucleotide metabolism.

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

The family also includes a group of related bacterial proteins of unknown function, see examples Q57843 and P76143.

Structural links Help

PDB - click here

SCOP: c.1.10.1

CATH: 3.20.20.70

Database links Help

Enzyme: EC:4.1.2

PANDIT: PF01791

Blocks: IPB002915

Pfam Clan: CL0036.20

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002915

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 Help

Additional Reading Open in usermanual
	Rosey EL, Oskouian B, Stewart GC. Lactose metabolism by Staphylococcus aureus: characterization of lacABCD, the structural genes of the tagatose 6-phosphate pathway. J. Bacteriol. 173 1991 5992-8 [PubMed: 1655695] http://jb.asm.org/cgi/content/abstract/173/19/5992
	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
	Sgarrella F, Del Corso A, Tozzi MG, Camici M. Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties. Biochim. Biophys. Acta 1118 1992 130-3 [PubMed: 1730028] http://dx.doi.org/10.1016/0167-4838(92)90139-5
	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
	Lorentzen E, Siebers B, Hensel R, Pohl E. Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates. Biochemistry 44 2005 4222-9 [PubMed: 15766250] http://dx.doi.org/10.1021/bi048192o
	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 2004 1816-23 [PubMed: 15388928] http://dx.doi.org/10.1107/S0907444904020190

InterPro 23.1