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InterPro: IPR006163 Phosphopantetheine-binding

Protein matches Help

UniProtKB

Matches:

11064 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

IPR006163 Phsphopanteth_bd

Secondary

IPR000255 , IPR003880

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00550	PP-binding	11064
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009081 Acyl carrier protein-like

Children

IPR003230 D-alanyl carrier protein
IPR003231 Acyl carrier protein (ACP)
IPR020806 Polyketide synthase, phosphopantetheine-binding

Found in

IPR004432 Polyketide-type polyunsaturated fatty acid synthase, PfaA
IPR014397 L-aminoadipate-semialdehyde dehydrogenase, large subunit
IPR016291 Isochorismatase, bacteria

Contains

IPR006162 Phosphopantetheine attachment site

GO Term annotation Help

Function

GO:0048037 cofactor binding

InterPro annotation

Entry Details in BioMart

Abstract

Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups [1].

The amino-terminal region of the ACP proteins is well defined and consists of alpha four helices arranged in a right-handed bundle held together by interhelical hydrophobic interactions. The Asp-Ser-Leu (DSL)motif is conserved in all of the ACP sequences, and the 4'-PP prosthetic group is covalently linked via a phosphodiester bond to the serine residue. The DSL sequence is present at the amino terminus of helix II, a domain of the protein referred to as the recognition helix and which is responsible for the interaction of ACPs with the enzymes of type II fatty acid synthesis [2].

Structural links Help

PDB - click here

SCOP: a.28.1.1 , a.28.1.2 , a.28.1.3 , e.23.1.1 , i.11.1.1

CATH: 1.10.1200.10

Database links Help

PROSITE doc: PDOC00012

PANDIT: PF00550

Blocks: IPB006163

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006163

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14561 Acyl carrier protein, mitochondrial

P07702 L-aminoadipate-semialdehyde dehydrogenase

P11829 Acyl carrier protein 1, chloroplastic

P19096 Fatty acid synthase

Q94519 Acyl carrier protein, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001227	Acyl transferase domain
IPR013149	Alcohol dehydrogenase, zinc-binding
IPR020843	Polyketide synthase, enoylreductase
IPR013120	Male sterility, NAD-binding
IPR020845	AMP-binding, conserved site
IPR016039	Thiolase-like
IPR014030	Beta-ketoacyl synthase, N-terminal
IPR016038	Thiolase-like, subgroup
IPR003231	Acyl carrier protein (ACP)
IPR018201	Beta-ketoacyl synthase, active site
IPR020842	Polyketide synthase/Fatty acid synthase, KR
IPR002198	Short-chain dehydrogenase/reductase SDR
IPR016036	Malonyl-CoA ACP transacylase, ACP-binding
IPR014031	Beta-ketoacyl synthase, C-terminal
IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase
IPR011032	GroES-like
IPR016040	NAD(P)-binding domain
IPR014397	L-aminoadipate-semialdehyde dehydrogenase, large subunit
IPR006162	Phosphopantetheine attachment site
IPR009081	Acyl carrier protein-like
IPR006163	Phosphopantetheine-binding
IPR010071	Amino acid adenylation
IPR000794	Beta-ketoacyl synthase
IPR000873	AMP-dependent synthetase/ligase
IPR014043	Acyl transferase
IPR010080	Thioester reductase
IPR001031	Thioesterase
IPR013217	Methyltransferase type 12
	ModBase
	SWISS-MODEL
	PDB Chain

Publications Open in usermanual
1.	Pugh EL, Wakil SJ. Studies on the mechanism of fatty acid synthesis. XIV. The prosthetic group of acyl carrier protein and the mode of its attachment to the protein. J. Biol. Chem. 240 4727-33 1965 [PubMed: 5321311] http://intl.jbc.org/cgi/reprint/240/12/4727.pdf
2.	Wong HC, Liu G, Zhang YM, Rock CO, Zheng J. The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 277 15874-80 2002 [PubMed: 11825906] http://dx.doi.org/10.1074/jbc.M112300200

Additional Reading Open in usermanual
	Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR. Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates. J. Mol. Biol. 365 2007 135-45 [PubMed: 17059829] http://dx.doi.org/10.1016/j.jmb.2006.09.049
	Zornetzer GA, Fox BG, Markley JL. Solution structures of spinach acyl carrier protein with decanoate and stearate. Biochemistry 45 2006 5217-27 [PubMed: 16618110] http://dx.doi.org/10.1021/bi052062d
	Cryle MJ, Schlichting I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc. Natl. Acad. Sci. U.S.A. 105 2008 15696-701 [PubMed: 18838690] http://dx.doi.org/10.1073/pnas.0805983105
	Ploskon E, Arthur CJ, Evans SE, Williams C, Crosby J, Simpson TJ, Crump MP. A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains. J. Biol. Chem. 283 2008 518-28 [PubMed: 17971456] http://dx.doi.org/10.1074/jbc.M703454200
	Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP. Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs. Biochemistry 45 2006 6904-16 [PubMed: 16734426] http://dx.doi.org/10.1021/bi060368u

InterPro 23.1