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InterPro: IPR003231 Acyl carrier protein (ACP)

Protein matchesHelp
UniProtKB
Matches:
2240 proteins
AccessionHelp IPR003231 Acyl_carrier
SecondaryHelp IPR003880
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR006163 Phosphopantetheine-binding
Contains IPR006162 Phosphopantetheine attachment site
GO Term annotationHelp
Process GO:0006633 fatty acid biosynthetic process
Function GO:0000036 acyl carrier activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

There are two types of fatty acid synthase systems. The type I system is found in metazoans and is carried out by a multifunctional polypeptide with multiple active sites. In contrast, the type II system found in bacteria and plants consists of a set of discrete monofunctional proteins, each encoded by a separate gene. ACP1 is central to both of these pathways because it functions to ferry the pathway intermediates between active site centres or enzymes. ACPs are also critical to the function of other metabolic pathways such as polyketide synthases.

The type II fatty acid synthase ACPs are abundant, small, acidic proteins that carry the acyl intermediates attached as thioesters to the terminus of the 4'-phosphopantetheine prosthetic group. This prosthetic group is added post-translationally to apoACP by holo-(acyl carrier protein) synthase (AcpS), which transfers the 4'-phosphopantetheine moiety of CoA to a serine reidue of apoACP.

The crystal structures of a number of the type II fatty acid synthase ACPs have been determined. The structures reveal a novel trimeric arrangement of molecules resulting in three active sites [1, 2].

Structural linksHelp
SCOP: a.28.1.1
CATH: 1.10.1200.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003231 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14561 Acyl carrier protein, mitochondrial

P11829 Acyl carrier protein 1, chloroplastic

P32463 Acyl carrier protein, mitochondrial

Q94519 Acyl carrier protein, mitochondrial

Q9CR21 Acyl carrier protein, mitochondrial

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR006162 Phosphopantetheine attachment site
IPR009081 Acyl carrier protein-like
IPR006163 Phosphopantetheine-binding
IPR003231 Acyl carrier protein (ACP)
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS.
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
Structure 8 883-95 2000 [PubMed: 10997907]
http://dx.doi.org/10.1016/S0969-2126(00)00178-7
2. Findlow SC, Winsor C, Simpson TJ, Crosby J, Crump MP.
Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus.
Biochemistry 42 8423-33 2003 [PubMed: 12859187]
http://dx.doi.org/10.1021/bi0342259

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
Rafi S, Novichenok P, Kolappan S, Zhang X, Stratton CF, Rawat R, Kisker C, Simmerling C, Tonge PJ.
Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli.
J. Biol. Chem. 281 2006 39285-93 [PubMed: 17012233]
http://dx.doi.org/10.1074/jbc.M608758200
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
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