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InterPro: IPR001980 Coenzyme A biosynthesis protein

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UniProtKB

Matches:

1607 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

IPR001980 LPS_biosynth

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00151	LPS_biosynth	1378
PRINTS	PR01020	LPSBIOSNTHSS	1605
TIGRFAMs	TIGR01510	coaD_prev_kdtB	1582
Signatures in BioMart

InterPro Relationships Help

Parent

IPR004820 Cytidylyltransferase

Contains

IPR004821 Cytidyltransferase-related

GO Term annotation Help

Process

GO:0015937 coenzyme A biosynthetic process

Function

GO:0004595 pantetheine-phosphate adenylyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

Temperature-sensitive mutants of Escherichia coli, defective in the transfer of 3-deoxy-D-manno-octulosonic acid (KDO) from CMP-KDO to a tetraacyldisaccharide 1,4'-bisphosphate precursor of lipid A, have been used to map KDO transferase activity on the E. coli chromosome [1]. The KDO transferase gene, designated kdtA, was shown to code for a 43kDa polypeptide. Overexpression of this single gene product greatly stimulates incorporation of two stereochemically distinct KDO residues during lipopolysaccharide biosynthesis in extracts of E. coli [1].

From these experiments this protein was thought to play a role in lipopolysaccharide biosynthesis, however now it is annotated as phosphopantetheine adenylyltransferase (EC:2.7.7.3), which catalyses the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine to give dephospho-CoA (DPCOA) and pyrophosphate in the fourth (and penultimate) step of coenzyme A biosynthesis [2].

Structural links Help

PDB - click here

SCOP: c.26.1.3

CATH: 3.40.50.620

Database links Help

Enzyme: EC:2.7.7.3

Blocks: IPB001980

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001980

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2BR50 Phosphopantetheine adenylyltransferase

O34797 Phosphopantetheine adenylyltransferase

Q55435 Phosphopantetheine adenylyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR001980	Coenzyme A biosynthesis protein
IPR004821	Cytidyltransferase-related
IPR004820	Cytidylyltransferase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Clementz T, Raetz CR. A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing. J. Biol. Chem. 266 9687-96 1991 [PubMed: 2033061] http://intl.jbc.org/cgi/reprint/266/15/9687.pdf
2.	Geerlof A, Lewendon A, Shaw WV. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem. 274 27105-11 1999 [PubMed: 10480925] http://dx.doi.org/10.1074/jbc.274.38.27105

Additional Reading Open in usermanual
	Izard T. The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism. J. Mol. Biol. 315 2002 487-95 [PubMed: 11812124] http://dx.doi.org/10.1006/jmbi.2001.5272
	Takahashi H, Inagaki E, Fujimoto Y, Kuroishi C, Nodake Y, Nakamura Y, Arisaka F, Yutani K, Kuramitsu S, Yokoyama S, Yamamoto M, Miyano M, Tahirov TH. Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus. Acta Crystallogr. D Biol. Crystallogr. 60 2004 97-104 [PubMed: 14684898]
	Izard T. A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A. J. Bacteriol. 185 2003 4074-80 [PubMed: 12837781] http://dx.doi.org/10.1128/JB.185.14.4074-4080.2003
	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
	Morris VK, Izard T. Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase. Protein Sci. 13 2004 2547-52 [PubMed: 15322293] http://dx.doi.org/10.1110/ps.04816904
	Roncero C, Casadaban MJ. Genetic analysis of the genes involved in synthesis of the lipopolysaccharide core in Escherichia coli K-12: three operons in the rfa locus. J. Bacteriol. 174 1992 3250-60 [PubMed: 1577693] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1577693

InterPro 23.1