EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR006269 3-deoxy-8-phosphooctulonate synthase

Protein matches Help

UniProtKB

Matches:

974 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

IPR006269 KDO8P_synthase

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00056	KDO8P_synthase	768
PANTHER	PTHR21057:SF2	KDO8P_synthase	966
TIGRFAMs	TIGR01362	KDO8P_synth	961
Signatures in BioMart

InterPro Relationships Help

Contains

IPR006218 DAHP synthetase I/KDSA

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0008676 3-deoxy-8-phosphooctulonate synthase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

These sequences describe 2-dehydro-3-deoxyphosphooctonate aldolase. Alternate names include 3-deoxy-d-manno-octulosonic acid 8-phosphate and KDO-8 phosphate synthetase. It catalyzes the aldol condensation of phosphoenolpyruvate with D-arabinose 5-phosphate.

phosphoenolpyruvate + D-arabinose 5-phosphate + H₂O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate

In Gram-negative bacteria, this is the first step in the biosynthesis of 3-deoxy-D-manno-octulosonate, part of the oligosaccharide core of lipopolysaccharide.

Structural links Help

PDB - click here

SCOP: c.1.10.4

CATH: 3.20.20.70

Database links Help

Enzyme: EC:2.5.1.55

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006269

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A5F692 2-dehydro-3-deoxyphosphooctonate aldolase

A5GI92 2-dehydro-3-deoxyphosphooctonate aldolase

O50044 2-dehydro-3-deoxyphosphooctonate aldolase

Q9AV97 2-dehydro-3-deoxyphosphooctonate aldolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR006218	DAHP synthetase I/KDSA
IPR006269	3-deoxy-8-phosphooctulonate synthase
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Help

Additional Reading Open in usermanual
	Xu X, Kona F, Wang J, Lu J, Stemmler T, Gatti DL. The catalytic and conformational cycle of Aquifex aeolicus KDO8P synthase: role of the L7 loop. Biochemistry 44 2005 12434-44 [PubMed: 16156656] http://dx.doi.org/10.1021/bi051095q
	Kona F, Xu X, Martin P, Kuzmic P, Gatti DL. Structural and mechanistic changes along an engineered path from metallo to nonmetallo 3-deoxy-D-manno-octulosonate 8-phosphate synthases. Biochemistry 46 2007 4532-44 [PubMed: 17381075] http://dx.doi.org/10.1021/bi6024879
	Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ. Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins 60 2005 787-96 [PubMed: 16021622] http://dx.doi.org/10.1002/prot.20541
	Kona F, Tao P, Martin P, Xu X, Gatti DL. Electronic structure of the metal center in the Cd(2+), Zn(2+), and Cu(2+) substituted forms of KDO8P synthase: implications for catalysis. Biochemistry 48 2009 3610-30 [PubMed: 19228070] http://dx.doi.org/10.1021/bi801955h
	Vainer R, Belakhov V, Rabkin E, Baasov T, Adir N. Crystal structures of Escherichia coli KDO8P synthase complexes reveal the source of catalytic irreversibility. J. Mol. Biol. 351 2005 641-52 [PubMed: 16023668] http://dx.doi.org/10.1016/j.jmb.2005.06.021

InterPro 23.1