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InterPro: IPR009081 Acyl carrier protein-like
Protein matches
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UniProtKB Matches: 13523 proteins |
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Accession
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IPR009081 Acyl_carrier_prot-like |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR006163 Phosphopantetheine-binding
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Found in
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IPR004432 Polyketide-type polyunsaturated fatty acid synthase, PfaA
IPR011407 10-formyltetrahydrofolate dehydrogenase
IPR014397 L-aminoadipate-semialdehyde dehydrogenase, large subunit
IPR016291 Isochorismatase, bacteria
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Contains
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IPR006162 Phosphopantetheine attachment site
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GO Term annotation
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Function
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GO:0000036 acyl carrier activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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].
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Structural links
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Example proteins
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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 |
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| IPR013149 |
Alcohol dehydrogenase, zinc-binding |
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| IPR020843 |
Polyketide synthase, enoylreductase |
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| IPR013120 |
Male sterility, NAD-binding |
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| IPR020845 |
AMP-binding, conserved site |
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| IPR016039 |
Thiolase-like |
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| IPR014030 |
Beta-ketoacyl synthase, N-terminal |
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| IPR016038 |
Thiolase-like, subgroup |
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| IPR003231 |
Acyl carrier protein (ACP) |
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| IPR018201 |
Beta-ketoacyl synthase, active site |
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| IPR020842 |
Polyketide synthase/Fatty acid synthase, KR |
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| IPR002198 |
Short-chain dehydrogenase/reductase SDR |
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| IPR016036 |
Malonyl-CoA ACP transacylase, ACP-binding |
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| IPR014031 |
Beta-ketoacyl synthase, C-terminal |
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| IPR016035 |
Acyl transferase/acyl hydrolase/lysophospholipase |
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| IPR011032 |
GroES-like |
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| IPR016040 |
NAD(P)-binding domain |
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| IPR014397 |
L-aminoadipate-semialdehyde dehydrogenase, large subunit |
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| IPR006162 |
Phosphopantetheine attachment site |
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| IPR009081 |
Acyl carrier protein-like |
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| IPR006163 |
Phosphopantetheine-binding |
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| IPR010071 |
Amino acid adenylation |
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| IPR000794 |
Beta-ketoacyl synthase |
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| IPR000873 |
AMP-dependent synthetase/ligase |
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| IPR014043 |
Acyl transferase |
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| IPR010080 |
Thioester reductase |
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| IPR001031 |
Thioesterase |
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| IPR013217 |
Methyltransferase type 12 |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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Publications
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1.
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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
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2.
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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
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3.
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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
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4.
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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
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Additional Reading
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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
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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
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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
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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
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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
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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
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InterPro 23.1
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