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InterPro: IPR014043 Acyl transferase

Protein matches Help

UniProtKB

Matches:

5909 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

IPR014043 Acyl_transferase

Secondary

IPR001227

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00698	Acyl_transf_1	5909
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001227 Acyl transferase domain

Children

IPR004410 Malonyl CoA-acyl carrier protein transacylase
IPR020801 Polyketide synthase, acyl transferase domain

Found in

IPR000794 Beta-ketoacyl synthase
IPR004432 Polyketide-type polyunsaturated fatty acid synthase, PfaA
IPR016452 Fatty acid synthase, beta subunit, fungi
IPR017554 Malonate decarboxylase, epsilon subunit

Contains

IPR016036 Malonyl-CoA ACP transacylase, ACP-binding

InterPro annotation

Entry Details in BioMart

Abstract

Enzymes like bacterial malonyl CoA-acly carrier protein transacylase (EC:2.3.1.39) and eukaryotic fatty acid synthase (EC:2.3.1.85) that are involved in fatty acid biosynthesis belong to this group. Also included are the polyketide synthases 6-methylsalicylic acid synthase (EC:2.3.1), a multifunctional enzyme that involved in the biosynthesis of patulin and conidial green pigment synthase (EC:2.3.1).

Structural links Help

PDB - click here

SCOP: c.19.1.1 , d.58.23.1

CATH: 3.30.70.250 , 3.40.366.10

Database links Help

Enzyme: EC:2.3.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR014043

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P07149

P19096

P49327

P73242

Q8T3L6

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001227	Acyl transferase domain
IPR003965	Fatty acid synthase
IPR013149	Alcohol dehydrogenase, zinc-binding
IPR020843	Polyketide synthase, enoylreductase
IPR016039	Thiolase-like
IPR016038	Thiolase-like, subgroup
IPR014030	Beta-ketoacyl synthase, N-terminal
IPR018201	Beta-ketoacyl synthase, active site
IPR016036	Malonyl-CoA ACP transacylase, ACP-binding
IPR020842	Polyketide synthase/Fatty acid synthase, KR
IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase
IPR014031	Beta-ketoacyl synthase, C-terminal
IPR011032	GroES-like
IPR013565	Domain of unknown function DUF1729
IPR016040	NAD(P)-binding domain
IPR004410	Malonyl CoA-acyl carrier protein transacylase
IPR006162	Phosphopantetheine attachment site
IPR002539	MaoC-like dehydratase
IPR009081	Acyl carrier protein-like
IPR006163	Phosphopantetheine-binding
IPR000794	Beta-ketoacyl synthase
IPR014043	Acyl transferase
IPR016452	Fatty acid synthase, beta subunit, fungi
IPR001031	Thioesterase
IPR013968	Polyketide synthase, KR
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Keatinge-Clay AT, Shelat AA, Savage DF, Tsai SC, Miercke LJ, O'Connell JD 3rd, Khosla C, Stroud RM. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure 11 2003 147-54 [PubMed: 12575934] http://dx.doi.org/10.1016/S0969-2126(03)00004-2
	Zhang L, Liu W, Xiao J, Hu T, Chen J, Chen K, Jiang H, Shen X. Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein. Protein Sci. 16 2007 1184-92 [PubMed: 17525466] http://dx.doi.org/10.1110/ps.072757307
	Oefner C, Schulz H, D'Arcy A, Dale GE. Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 62 2006 613-8 [PubMed: 16699188] http://dx.doi.org/10.1107/S0907444906009474
	Serre L, Verbree EC, Dauter Z, Stuitje AR, Derewenda ZS. The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component. J. Biol. Chem. 270 1995 12961-4 [PubMed: 7768883] http://dx.doi.org/10.1074/jbc.270.22.12961

InterPro 24.0