pssA

UniProt ID: Q88GQ4
Organism: Pseudomonas putida KT2440
Review Status: COMPLETE
Aliases:
PP_3664
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Gene Description

pssA (PP_3664) encodes CDP-diacylglycerol--serine O-phosphatidyltransferase, the phosphatidylserine synthase that catalyzes the first of two consecutive reactions in the major bacterial phosphatidylethanolamine pathway. It transfers the phosphatidyl group of CDP-diacylglycerol to L-serine to form phosphatidylserine, which is then decarboxylated by Psd.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003824 catalytic activity
IEA
GO_REF:0000002
TOO GENERAL
Summary: Generic catalytic activity is true but provides no information beyond the specific phosphatidyltransferase term.
Reason: True, but entailed by GO:0003882 CDP-diacylglycerol-serine O-phosphatidyltransferase activity, accepted in this review.
Supporting Evidence:
file:PSEPK/pssA/pssA-uniprot.txt
DR PIRSF; PIRSF000850; Phospholipase_D_PSS; 1.
GO:0003882 CDP-diacylglycerol-serine O-phosphatidyltransferase activity
IEA
GO_REF:0000120
ACCEPT
Summary: Combined electronic annotation (EC mapping plus TreeGrafter placement at the PAINT phosphatidylserine-synthase node PTN001758495). Q88GQ4 carries the PssA-specific NCBIfam and PIRSF signatures, and its type-I ortholog in E. coli is the biochemically characterized phosphatidylserine synthase.
Reason: This is the specific core molecular function of PssA.
Supporting Evidence:
file:PSEPK/pssA/pssA-uniprot.txt
DR NCBIfam; NF006946; PRK09428.1; 1.
file:PSEPK/pssA/pssA-uniprot.txt
DR PIRSF; PIRSF000850; Phospholipase_D_PSS; 1.
PMID:39693441
Type I PssA belongs to the phospholipase D (PLD) superfamily
file:PSEPK/pssA/pssA-deep-research-openscientist.md
The core function of PP_3664 is synthesis of phosphatidylserine as the obligatory precursor of phosphatidylethanolamine.
GO:0005737 cytoplasm
IEA
GO_REF:0000117
TOO GENERAL
Summary: PssA lacks transmembrane helices, but cytoplasm is redundant with the more specific cytosol annotation.
Reason: True, but entailed by GO:0005829 cytosol, kept in this review; the active location is the cytoplasmic face of the inner membrane (GO:0005886).
Supporting Evidence:
PMID:39693441
A peripheral membrane protein PssA can associate with the cellular membrane in its active state or exist in the cytosol in an inactive form.
GO:0005829 cytosol
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: The soluble/peripheral phosphatidylserine synthase is assigned to the cytosol by TreeGrafter.
Reason: Retain the soluble-state location, but do not use it as the core catalytic location because type-I PssA is active at the membrane surface.
Supporting Evidence:
PMID:39693441
the active state of PssA is associated with the inner membrane surface, contributing to PS synthesis, while the cytosolic form is inactive in this synthesis process
GO:0005886 plasma membrane
ISS
PMID:39693441
Structural basis for membrane association and catalysis by p...
NEW
Summary: Type-I PssA carries out phosphatidylserine synthesis while peripherally associated with the cytoplasmic face of the inner membrane.
Reason: The experimentally characterized E. coli type-I ortholog is active at the inner membrane surface, and Q88GQ4 has the same PLD-superfamily architecture.
Supporting Evidence:
PMID:39693441
the active state of PssA is associated with the inner membrane surface, contributing to PS synthesis, while the cytosolic form is inactive in this synthesis process
GO:0008444 CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity
IEA
GO_REF:0000002
REMOVE
Summary: This is phosphatidylglycerophosphate synthase activity, using glycerol-3-phosphate rather than serine, and is a distinct enzyme reaction.
Reason: PssA is assigned EC 2.7.8.8 and GO:0003882. GO:0008444 corresponds to the PgsA reaction and conflicts with the protein name and substrate specificity; the InterPro mapping has over-propagated a different phospholipid-synthase activity.
Supporting Evidence:
file:ECOLI/pssA/pssA-uniprot.txt
Catalyzes the conversion of cytidine diphosphate diacylglycerol (CDP-DG) and L-serine into phosphatidylserine (PubMed:39693441, PubMed:8824831).
file:PSEPK/pssA/pssA-notes.md
PssA uses L-serine to form phosphatidylserine; GO:0008444 instead denotes transfer to glycerol-3-phosphate.
GO:0032049 cardiolipin biosynthetic process
IEA
GO_REF:0000002
REMOVE
Summary: Cardiolipin biosynthesis proceeds through phosphatidylglycerol and cardiolipin synthase, not through the PssA phosphatidylserine reaction.
Reason: This process annotation is inherited from the same inappropriate phosphatidylglycerol/cardiolipin family mapping as GO:0008444. PssA instead supplies phosphatidylserine to Psd for phosphatidylethanolamine biosynthesis; in the E. coli type-I ortholog, loss of PssA raises rather than lowers phosphatidylglycerol and cardiolipin.
Supporting Evidence:
PMID:179992
while the combined levels of phosphatidylglycerol and cardiolipin rise from 34 to 68%.
GO:0006646 phosphatidylethanolamine biosynthetic process
IC
file:PSEPK/pssA/pssA-notes.md
NEW
Summary: PssA supplies phosphatidylserine to the terminal Psd reaction in phosphatidylethanolamine biosynthesis.
Reason: The accepted phosphatidylserine-synthase activity and consecutive PssA-Psd pathway support this missing process annotation.
Supporting Evidence:
file:PSEPK/pssA/pssA-notes.md
PssA forms phosphatidylserine, which is the substrate for the consecutive Psd decarboxylation reaction.

Core Functions

CDP-diacylglycerol--serine O-phosphatidyltransferase producing phosphatidylserine in the first step of phosphatidylethanolamine biosynthesis.

Supporting Evidence:
  • file:PSEPK/pssA/pssA-uniprot.txt
    DR NCBIfam; NF006946; PRK09428.1; 1.
  • file:PSEPK/pssA/pssA-notes.md
    PssA forms phosphatidylserine, which is the substrate for the consecutive Psd decarboxylation reaction.
  • file:PSEPK/pssA/pssA-deep-research-openscientist.md
    The core function of PP_3664 is synthesis of phosphatidylserine as the obligatory precursor of phosphatidylethanolamine.
  • PMID:39693441
    the active state of PssA is associated with the inner membrane surface, contributing to PS synthesis, while the cytosolic form is inactive in this synthesis process

References

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Deep Research

OpenScientist

(pssA-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(pssA-notes.md)

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