EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR001736 Phospholipase D/Transphosphatidylase

Protein matches Help

UniProtKB

Matches:

5159 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

IPR001736 PLipase_D/transphosphatidylase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00614	PLDc	4090
PROSITE profile	PS50035	PLD	5095
SMART	SM00155	PLDc	4207
Signatures in BioMart

InterPro Relationships Help

Found in

IPR011402 Phospholipase D, plant
IPR015679 Phospholipase D
IPR016270 Phospholipase D, phosphatidylserine synthase type
IPR016555 Phospholipase D, eukaryota
IPR016834 Uncharacterised conserved protein UCP026306

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

Phosphatidylcholine-hydrolysing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, and/or asparagine residues which may contribute to the active site aspartic acid. An Escherichia coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs [1, 2, 3, 4].

Structural links Help

PDB - click here

SCOP: d.136.1.1 , d.136.1.2 , d.136.1.4

CATH: 3.30.870.10

Database links Help

PROSITE doc: PDOC50035

PANDIT: PF00614

Blocks: IPB001736

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001736

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14939 Phospholipase D2

O17405 Probable phospholipase D F09G2.8

O23078 Phospholipase D beta 2

O35405 Phospholipase D3

P25578 CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001849	Pleckstrin homology
IPR011402	Phospholipase D, plant
IPR001736	Phospholipase D/Transphosphatidylase
IPR013582	Phospholipase D/viral envelope
IPR018029	C2 membrane targeting protein
IPR015679	Phospholipase D
IPR008973	C2 calcium/lipid-binding domain, CaLB
IPR000008	C2 calcium-dependent membrane targeting
IPR016555	Phospholipase D, eukaryota
IPR016270	Phospholipase D, phosphatidylserine synthase type
IPR001683	Phox-like
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Ponting CP, Kerr ID. A novel family of phospholipase D homologues that includes phospholipid synthases and putative endonucleases: identification of duplicated repeats and potential active site residues. Protein Sci. 5 914-22 1996 [PubMed: 8732763] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8732763&action=stream&blobtype=pdf
2.	Koonin EV. A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins. Trends Biochem. Sci. 21 242-3 1996 [PubMed: 8755242] http://dx.doi.org/10.1016/0968-0004(96)30024-8
3.	Wang X, Xu L, Zheng L. Cloning and expression of phosphatidylcholine-hydrolyzing phospholipase D from Ricinus communis L. J. Biol. Chem. 269 20312-7 1994 [PubMed: 8051126] http://intl.jbc.org/cgi/reprint/269/32/20312.pdf
4.	Singer WD, Brown HA, Sternweis PC. Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D. Annu. Rev. Biochem. 66 475-509 1997 [PubMed: 9242915] http://dx.doi.org/10.1146/annurev.biochem.66.1.475

Additional Reading Open in usermanual
	Xie Z, Ho WT, Exton JH. Association of the N- and C-terminal domains of phospholipase D. Contribution of the conserved HKD motifs to the interaction and the requirement of the association for Ser/Thr phosphorylation of the enzyme. J. Biol. Chem. 275 2000 24962-9 [PubMed: 10825182] http://dx.doi.org/10.1074/jbc.M909745199
	Leiros I, Secundo F, Zambonelli C, Servi S, Hough E. The first crystal structure of a phospholipase D. Structure 8 2000 655-67 [PubMed: 10873862] http://dx.doi.org/10.1016/S0969-2126(00)00150-7
	Masayama A, Takahashi T, Tsukada K, Nishikawa S, Takahashi R, Adachi M, Koga K, Suzuki A, Yamane T, Nakano H, Iwasaki Y. Streptomyces phospholipase D mutants with altered substrate specificity capable of phosphatidylinositol synthesis. Chembiochem 9 2008 974-81 [PubMed: 18338352] http://dx.doi.org/10.1002/cbic.200700528
	Leiros I, McSweeney S, Hough E. The reaction mechanism of phospholipase D from Streptomyces sp. strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product. J. Mol. Biol. 339 2004 805-20 [PubMed: 15165852] http://dx.doi.org/10.1016/j.jmb.2004.04.003
	Zhu Y, Huang W, Lee SS, Xu W. Crystal structure of a polyphosphate kinase and its implications for polyphosphate synthesis. EMBO Rep. 6 2005 681-7 [PubMed: 15947782] http://dx.doi.org/10.1038/sj.embor.7400448
	Stuckey JA, Dixon JE. Crystal structure of a phospholipase D family member. Nat. Struct. Biol. 6 1999 278-84 [PubMed: 10074947] http://dx.doi.org/10.1038/6716
	Morris AJ, Engebrecht J, Frohman MA. Structure and regulation of phospholipase D. Trends Pharmacol. Sci. 17 1996 182-5 [PubMed: 8669123] http://dx.doi.org/10.1016/0165-6147(96)10016-X

InterPro 23.1