spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR009081 Acyl carrier protein-like

Protein matchesHelp
UniProtKB
Matches:
13523 proteins
AccessionHelp IPR009081 Acyl_carrier_prot-like
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR006163 Phosphopantetheine-binding
Found in IPR004432 Polyketide-type polyunsaturated fatty acid synthase, PfaA
IPR011407 10-formyltetrahydrofolate dehydrogenase
IPR014397 L-aminoadipate-semialdehyde dehydrogenase, large subunit
IPR016291 Isochorismatase, bacteria
Contains IPR006162 Phosphopantetheine attachment site
GO Term annotationHelp
Function GO:0000036 acyl carrier activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Acyl carrier protein (ACP) is an essential cofactor in the synthesis of fatty acids by the fatty acid synthetases systems in bacteria and plants. In addition to fatty acid synthesis, ACP is also involved in many other reactions that require acyl transfer steps, such as the synthesis of polyketide antibiotics, biotin precursor, membrane-derived oligosaccharides, and activation of toxins, and functions as an essential cofactor in lipoylation of pyruvate and alpha-ketoglutarate dehydrogenase complexes [1]. 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 [2]. Phosphopantetheine is attached to a serine residue in these proteins. The core structure of ACP consists of a four-helical bundle, where helix three is shorter than the others.

Several other proteins share structural homology with ACP, such as the bacterial apo-D-alanyl carrier protein, which facilitates the incorporation of D-alanine into lipoteichoic acid by a ligase, necessary for the growth and development of Gram-positive organisms [3]; and the thioester domain of the bacterial peptide carrier protein (PCP) found within large modular non-ribosomal peptide synthetases, which are responsible for the synthesis of a variety of microbial bioactive peptides [4].

Structural linksHelp
CATH: 1.10.1200.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR009081 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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

PublicationsHelp
1. Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB.
X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site.
Structure 10 825-35 2002 [PubMed: 12057197]
http://dx.doi.org/10.1016/S0969-2126(02)00775-X
2. Crawford JM, Vagstad AL, Ehrlich KC, Udwary DW, Townsend CA.
Acyl-carrier protein-phosphopantetheinyltransferase partnerships in fungal fatty acid synthases.
Chembiochem 9 1559-63 2008 [PubMed: 18551496]
http://dx.doi.org/10.1002/cbic.200700659
3. Volkman BF, Zhang Q, Debabov DV, Rivera E, Kresheck GC, Neuhaus FC.
Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein.
Biochemistry 40 7964-72 2001 [PubMed: 11434765]
http://dx.doi.org/10.1021/bi010355a
4. Weber T, Baumgartner R, Renner C, Marahiel MA, Holak TA.
Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases.
Structure 8 407-18 2000 [PubMed: 10801488]
http://dx.doi.org/10.1016/S0969-2126(00)00120-9

Additional ReadingHelp
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
Witkowski A, Rangan VS, Randhawa ZI, Amy CM, Smith S.
Structural organization of the multifunctional animal fatty-acid synthase.
Eur. J. Biochem. 198 1991 571-9 [PubMed: 2050137]
http://dx.doi.org/10.1111/j.1432-1033.1991.tb16052.x
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
spacer
spacer
InterPro 23.1