Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
[Rab1 protein]-O-phosphocholine-L-serine
Identifier
RHEA-COMP:14085
Reactive part
help_outline
- Name help_outline O-phosphocholine-L-serine residue Identifier CHEBI:138595 Charge 0 Formula C8H17N2O5P SMILEShelp_outline C(*)(=O)[C@H](COP(OCC[N+](C)(C)C)(=O)[O-])N* 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[Rab1 protein]-L-serine
Identifier
RHEA-COMP:14376
Reactive part
help_outline
- Name help_outline L-serine residue Identifier CHEBI:29999 Charge 0 Formula C3H5NO2 SMILEShelp_outline C([C@H](CO)N*)(=O)* 2D coordinates Mol file for the small molecule Search links Involved in 72 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphocholine Identifier CHEBI:295975 Charge -1 Formula C5H13NO4P InChIKeyhelp_outline YHHSONZFOIEMCP-UHFFFAOYSA-M SMILEShelp_outline C[N+](C)(C)CCOP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 35 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 10,232 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56084 | RHEA:56085 | RHEA:56086 | RHEA:56087 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination.
Tan Y., Arnold R.J., Luo Z.Q.
Effectors delivered into host cells by the Legionella pneumophila Dot/Icm type IV transporter are essential for the biogenesis of the specialized vacuole that permits its intracellular growth. The biochemical function of most of these effectors is unknown, making it difficult to assign their roles ... >> More
Effectors delivered into host cells by the Legionella pneumophila Dot/Icm type IV transporter are essential for the biogenesis of the specialized vacuole that permits its intracellular growth. The biochemical function of most of these effectors is unknown, making it difficult to assign their roles in the establishment of successful infection. We found that several yeast genes involved in membrane trafficking, including the small GTPase Ypt1, strongly suppress the cytotoxicity of Lpg0695(AnkX), a protein known to interfere severely with host vesicle trafficking when overexpressed. Mass spectrometry analysis of Rab1 purified from a yeast strain inducibly expressing AnkX revealed that this small GTPase is modified posttranslationally at Ser(76) by a phosphorylcholine moiety. Using cytidine diphosphate-choline as the donor for phosphorylcholine, AnkX catalyzes the transfer of phosphorylcholine to Rab1 in a filamentation-induced by cAMP(Fic) domain-dependent manner. Further, we found that the activity of AnkX is regulated by the Dot/Icm substrate Lpg0696(Lem3), which functions as a dephosphorylcholinase to reverse AnkX-mediated modification on Rab1. Phosphorylcholination interfered with Rab1 activity by making it less accessible to the bacterial GTPase activation protein LepB; this interference can be alleviated fully by Lem3. Our results reveal reversible phosphorylcholination as a mechanism for balanced modulation of host cellular processes by a bacterial pathogen. << Less
Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011) [PubMed] [EuropePMC]