The domain within your query sequence starts at position 499 and ends at position 551; the E-value for the PlsC domain shown below is 8e-27.

WARNING!
Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 11377195 ) for details.

Catalytic residues
Position		Amino acid	Present?
Domain	Protein
N/A	N/A	H	No
N/A	N/A	D	No

GIHLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCVTITHTSR

The domain was found using the schnipsel database

PlsC

Phosphate acyltransferases

• SMART accession number: SM00563
• Description: Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.
• Interpro abstract (IPR002123):

  This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function [ (PUBMED:9259571) ]. This domain is found in tafazzins, defects in which are the cause of Barth syndrome; a severe inherited disorder which is often fatal in childhood and is characterised by cardiac and skeletal abnormalities. Phospholipid/glycerol acyltransferase is not found in the viruses or the archaea and is under represented in the bacteria. Bacterial glycerol-phosphate acyltransferases are involved in membrane biogenesis since they use fatty acid chains to form the first membrane phospholipids [ (PUBMED:18369234) ].

• GO function: transferase activity, transferring acyl groups (GO:0016746)

There are 106677 PlsC domains in 106607 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Neuwald AF
• Barth syndrome may be due to an acyltransferase deficiency.
• Curr Biol. 1997; 7: 4656-4656

Disease (disease genes where sequence variants are found in this domain)

SwissProt sequences and OMIM curated human diseases associated with missense mutations within the PlsC domain.

Protein	Disease
Dihydroxyacetone phosphate acyltransferase (O15228) (SMART)	OMIM:602744: Chondrodysplasia punctata, rhizomelic, type 2 OMIM:222765:

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
30.90	map00564	Glycerophospholipid metabolism
28.95	map00561	Glycerolipid metabolism
23.33	map00565	Ether lipid metabolism
2.79	map00071	Fatty acid metabolism
1.44	map00350	Tyrosine metabolism
1.44	map00903	Limonene and pinene degradation
1.44	map00960	Alkaloid biosynthesis II
1.44	map00310	Lysine degradation
1.44	map00340	Histidine metabolism
1.44	map00360	Phenylalanine metabolism
1.44	map00624	1- and 2-Methylnaphthalene degradation
1.44	map00642	Ethylbenzene degradation
1.44	map00632	Benzoate degradation via CoA ligation
0.23	map03320	PPAR signaling pathway
0.23	map04920	Adipocytokine signaling pathway
0.23	map00540	Lipopolysaccharide biosynthesis
0.09	map01031	Glycan structures - biosynthesis 2
0.05	map00232	Caffeine metabolism
0.05	map00650	Butanoate metabolism
0.05	map00620	Pyruvate metabolism
0.05	map00563	Glycosylphosphatidylinositol(GPI)-anchor biosynthesis
0.05	map00640	Propanoate metabolism
0.05	map00633	Trinitrotoluene degradation

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with PlsC domain which could be assigned to a KEGG orthologous group, and not all proteins containing PlsC domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of PlsC domains in PDB

PDB code	Title
1iuq	The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase
1k30	Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase

Links (links to other resources describing this domain)

• INTERPRO: IPR002123