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InterPro: IPR008278 4'-phosphopantetheinyl transferase

Protein matchesHelp
UniProtKB
Matches:
3164 proteins
AccessionHelp IPR008278 4-PPantetheinyl_Trfase
SecondaryHelp IPR002582 , IPR004568
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004568 Phosphopantethiene-protein transferase
IPR016614 Holo-[acyl-carrier-protein] synthase, fungi
Found in IPR003542 Enterobactin synthetase-like, component D
GO Term annotationHelp
Process GO:0009059 macromolecule biosynthetic process
Function GO:0000287 magnesium ion binding
GO:0008897 holo-[acyl-carrier-protein] synthase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

These proteins transfer the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pp-binding. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP [1]. This superfamily consists of two subtypes: The ACPS type such as ACPS_ECOLI and the Sfp type such as SFP_BACSU. The structure of the Sfp type is known [2], which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.

Structural linksHelp
CATH: 3.90.470.20
Database linksHelp
Enzyme: EC:2.7.8.7
PANDIT: PF01648
Blocks: IPB008278

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008278 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O86785 Holo-[acyl-carrier-protein] synthase

P19097 Fatty acid synthase subunit alpha

Q55185 Putative 4'-phosphopantetheinyl transferase slr0495

Q9CQF6 L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase

Q9NRN7 L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001227 Acyl transferase domain
IPR016039 Thiolase-like
IPR014030 Beta-ketoacyl synthase, N-terminal
IPR016038 Thiolase-like, subgroup
IPR018201 Beta-ketoacyl synthase, active site
IPR014031 Beta-ketoacyl synthase, C-terminal
IPR008278 4'-phosphopantetheinyl transferase
IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase
IPR004568 Phosphopantethiene-protein transferase
IPR016040 NAD(P)-binding domain
IPR000794 Beta-ketoacyl synthase
IPR002582 Holo-[acyl carrier protein] synthase
PDB Chain
ModBase
CATH Domain
SWISS-MODEL

PublicationsHelp
1. Lambalot RH, Walsh CT.
Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase.
J. Biol. Chem. 270 24658-61 1995 [PubMed: 7559576]
http://dx.doi.org/10.1074/jbc.270.42.24658
2. Reuter K, Mofid MR, Marahiel MA, Ficner R.
Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily.
EMBO J. 18 6823-31 1999 [PubMed: 10581256]
http://dx.doi.org/10.1093/emboj/18.23.6823

Additional ReadingHelp
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 2000 883-95 [PubMed: 10997907]
http://dx.doi.org/10.1016/S0969-2126(00)00178-7
Chirgadze NY, Briggs SL, McAllister KA, Fischl AS, Zhao G.
Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis.
EMBO J. 19 2000 5281-7 [PubMed: 11032795]
http://dx.doi.org/10.1093/emboj/19.20.5281
Lambalot RH, Gehring AM, Flugel RS, Zuber P, LaCelle M, Marahiel MA, Reid R, Khosla C, Walsh CT.
A new enzyme superfamily - the phosphopantetheinyl transferases.
Chem. Biol. 3 1996 923-36 [PubMed: 8939709]
http://dx.doi.org/10.1016/S1074-5521(96)90181-7
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InterPro 23.1