AGRT5:A9CIM3

Species (Taxon ID)	Agrobacterium tumefaciens (strain C58 / ATCC 33970). (176299)
Gene Name(s)	pcs
Protein Name(s)	Phosphatidylcholine synthase
External Links
UniProt	A9CIM3
EMBL	AE007869
RefSeq	NP_354778.2
ProteinModelPortal	A9CIM3
STRING	176299.Atu1793
EnsemblBacteria	AAK87563
GeneID	1133831
KEGG	atu:Atu1793
PATRIC	20813363
eggNOG	COG1183
HOGENOM	HOG000066428
KO	K01004
OMA	FLHPFRV
OrthoDB	EOG6P5ZJN
ProtClustDB	CLSK863002
GO	GO:0016020 GO:0016780 GO:0008654
InterPro	IPR000462 IPR026027
Pfam	PF01066
PIRSF	PIRSF000851

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0008654	phospholipid biosynthetic process	PMID:2612428	ECO:0000314			P		Figure 2B shows that Phosphatidylcholine synthase uses choline to directly synthesize PC. Figure 2 (A&B) shows that Pcs is active when expressed and is likely responsible for PC synthesis without the requirement of additional proteins.	complete
	GO:0072657	protein localization to membrane	PMID:2612428	ECO:0000314			P		Figure 6 shows that A. tumefaciens has significant levels of PC in both the inner and outer membranes, indicating Pcs activity in these locations.	complete
	GO:0048870	cell motility	PMID:2612428	ECO:0000315			P		Figure 7 shows that A. tumefaciens is highly motile, and that the motility of the pmtA/pcs double mutant was greatly decreased. This figure also showed that when the pcs mutant was complimented with pcs expressed from a low copy number vector, motility was partially restored.	complete
	GO:0042710	biofilm formation	PMID:2612428	ECO:0000315			P		Figure 8 shows that a PC-deficient double mutant (pcs/pmtA) formed thicker and more dense communities in comparison to wild type. It shows that there were numerous large, towering structures present.	complete
enables	GO:0050520	phosphatidylcholine synthase activity		ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0050520	phosphatidylcholine synthase activity		ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008654	phospholipid biosynthetic process		ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008654	phospholipid biosynthetic process		ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding		ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:A9CIM3	F		Seeded From UniProt	complete
enables	GO:0050520	phosphatidylcholine synthase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.8.24	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0997 UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0037	C		Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P		Seeded From UniProt	complete
involved_in	GO:0008654	phospholipid biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0594	P		Seeded From UniProt	complete
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References

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