gcvP1

UniProt ID: Q88P65
Organism: Pseudomonas putida KT2440
Review Status: COMPLETE
Aliases:
PP_0988 gcvP-1
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Gene Description

GcvP1 is one of two KT2440 glycine cleavage P proteins. It is a PLP-dependent glycine dehydrogenase that decarboxylates glycine and transfers the remaining aminomethyl group to the covalently lipoylated H protein. Together with GcvH1 and GcvT-I, it forms one of two paralogous P/H/T sets that can implement the glycine cleavage cycle with a shared dihydrolipoyl dehydrogenase.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004375 glycine dehydrogenase (decarboxylating) activity
IEA
GO_REF:0000120 		ACCEPT
Summary: This is the defining PLP-dependent P-protein reaction.
Reason: UniProt assigns EC 1.4.4.2 and Rhea 24304, and describes transfer of the glycine-derived aminomethyl group to H protein.
Supporting Evidence:
file:PSEPK/gcvP1/gcvP1-uniprot.txt
The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein
GO:0005829 cytosol
IEA
GO_REF:0000118 		KEEP AS NON CORE
Summary: A soluble cytoplasmic location is plausible but does not define GcvP1 function.
Reason: This TreeGrafter row descends from the PTHR11773 PAINT node PTN000206531, whose cytosol IBD is seeded by E. coli GcvP (P33195). KT2440 GcvP1 is a bacterial protein with no signal peptide or transmembrane feature in the record, so the soluble cytoplasmic location holds; it is retained as non-core context for the catalytic role.
Supporting Evidence:
file:interpro/panther/PTHR11773/PTHR11773-paint.tsv
PTHR11773 PTN000206531 GO:0005829 C IBD false UniProtKB:P33195
GO:0005960 glycine cleavage complex
IEA
GO_REF:0000118 		ACCEPT
Summary: GcvP1 is the P component of a four-protein glycine cleavage system.
Reason: The reviewed UniProt record explicitly identifies P, H, T, and L proteins as system components.
Supporting Evidence:
file:PSEPK/gcvP1/gcvP1-uniprot.txt
The glycine cleavage system is composed of four proteins: P, T, L and H.
GO:0006544 glycine metabolic process
IEA
GO_REF:0000002 		MODIFY
Summary: True but broad parent of the glycine cleavage process.
Reason: Correct but general: glycine metabolic process is an ancestor of GO:0019464 glycine decarboxylation via glycine cleavage system, which this gene already carries and which is the process the gene product directly performs a step of. MODIFY to that descendant; applied the same way to every P-, H-, T- and L-protein review in the glycine cleavage system module.
Supporting Evidence:
file:PSEPK/gcvP1/gcvP1-uniprot.txt
The glycine cleavage system catalyzes the degradation of glycine.
GO:0006546 glycine catabolic process
IEA
GO_REF:0000002 		MODIFY
Summary: True but broad parent of the glycine cleavage process.
Reason: Correct but general: glycine catabolic process is an ancestor of GO:0019464 glycine decarboxylation via glycine cleavage system, which this gene already carries and which is the process the gene product directly performs a step of. MODIFY to that descendant; applied the same way to every P-, H-, T- and L-protein review in the glycine cleavage system module.
Supporting Evidence:
file:PSEPK/gcvP1/gcvP1-uniprot.txt
The glycine cleavage system catalyzes the degradation of glycine.
GO:0016594 glycine binding
IEA
GO_REF:0000118 		KEEP AS NON CORE
Summary: Glycine binding is a genuine substrate interaction but is ancillary to the catalytic activity.
Reason: Glycine binding is a true substrate interaction, while GO:0004375 remains the informative core catalytic term.
Supporting Evidence:
file:PSEPK/gcvP1/gcvP1-uniprot.txt
The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor
GO:0019464 glycine decarboxylation via glycine cleavage system
IEA
GO_REF:0000120 		ACCEPT
Summary: GcvP1 performs the initiating reaction of this exact process.
Reason: The UniProt function and exact Rhea reaction place GcvP1 directly in the glycine cleavage cycle.
Supporting Evidence:
file:PSEPK/gcvP1/gcvP1-uniprot.txt
The glycine cleavage system catalyzes the degradation of glycine.
GO:0030170 pyridoxal phosphate binding
IEA
GO_REF:0000118 		KEEP AS NON CORE
Summary: PLP is the required P-protein cofactor but is ancillary to the catalytic function.
Reason: UniProt records PLP dependence; the catalytic activity remains the core molecular function.
Supporting Evidence:
file:PSEPK/gcvP1/gcvP1-uniprot.txt
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;

Core Functions

PLP-dependent glycine cleavage P protein that decarboxylates glycine and loads its aminomethyl group onto lipoyl-H protein.

Molecular Function:
glycine dehydrogenase (decarboxylating) activity
Directly Involved In:
glycine decarboxylation via glycine cleavage system
In Complex:
glycine cleavage complex
Supporting Evidence:
  • file:PSEPK/gcvP1/gcvP1-uniprot.txt
    The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein

References

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Suggested Questions for Experts

Q: Under which growth conditions is the gcvT-I/gcvP1/gcvH1 locus used relative to the second P/H/T set?

Suggested Experiments

Experiment: Compare glycine-dependent growth and operon expression in clean gcvP1 and gcvP2 single and double mutants.

Type: comparative genetics and expression analysis

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