glyA

UniProt ID: P50435
Organism: Methylorubrum extorquens AM1
Review Status: COMPLETE
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Gene Description

glyA encodes serine hydroxymethyltransferase (SHMT, EC 2.1.2.1), a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF). This reaction is crucial for the serine cycle, the central assimilatory pathway in methylotrophy, where it serves as the major source of one-carbon groups required for biosynthesis of purines, thymidylate, methionine, and other biomolecules. The enzyme functions as a homodimer in the cytoplasm. SHMT catalyzes: L-serine + THF β‡Œ glycine + 5,10-methylenetetrahydrofolate + Hβ‚‚O. In methylotrophic metabolism, this enzyme is essential for converting C1 units from formaldehyde oxidation (via the H4MPT pathway) into the tetrahydrofolate pool, where they are used for serine biosynthesis from glycine, completing a key step in the serine cycle. The enzyme also exhibits THF-independent aldolase activity toward Ξ²-hydroxyamino acids. Genetic studies (insertional inactivation in M. extorquens AM1) have confirmed glyA is essential for methylotrophic growth: glyA null mutants lose all detectable SHMT activity and cannot grow on C1 compounds (including methanol) even when supplemented with glycine or serine, while still growing normally on succinate. SHMT activity is ~6-fold induced on methanol versus succinate and has been flagged as a potential rate-limiting step in the serine cycle.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004372 glycine hydroxymethyltransferase activity
IEA
GO_REF:0000120
ACCEPT
Summary: Correct - SHMT catalyzes the reversible PLP-dependent interconversion of serine and glycine with THF as the one-carbon carrier; this is the core molecular function of glyA and is directly supported by organism-specific enzymology in M. extorquens AM1.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
catalyzes the reversible folate-linked one-carbon transfer between serine and glycine: **L-serine + tetrahydrofolate (THF) ⇄ glycine + 5,10-methylenetetrahydrofolate (5,10-CH2-THF) + H2O**
file:METEA/glyA/glyA-deep-research-falcon.md
Insertional inactivation of **glyA** in AM1 eliminates measurable SHMT activity and causes a strong growth defect on **C1 substrates**
GO:0005737 cytoplasm
IEA
GO_REF:0000120
ACCEPT
Summary: Correct - SHMT is a soluble cytosolic enzyme participating in the serine cycle; no membrane/periplasmic/secretion signal is present and AM1 activity is measured in cell extracts. No direct AM1 localization experiment exists, so this remains an inference from enzymology and conserved bacterial SHMT biology.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
all evidence places GlyA in intracellular folate/serine-cycle metabolism
GO:0005829 cytosol
IEA
GO_REF:0000118
ACCEPT
Summary: Correct - More specific than cytoplasm; SHMT operates as a soluble enzyme in the cytosolic compartment. As with cytoplasm, this is inferred from enzymology (activity in cell extracts) rather than a direct AM1 localization experiment.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
soluble cytosolic enzyme
GO:0006730 one-carbon metabolic process
IEA
GO_REF:0000043
ACCEPT
Summary: Correct - SHMT is the central node linking folate-bound one-carbon units to amino acid metabolism in the serine cycle, integrating C1 units derived from methanol/formaldehyde oxidation into biosynthesis.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
a key link between **folate-linked one-carbon metabolism** and assimilation of formaldehyde derived from methanol oxidation
GO:0008652 amino acid biosynthetic process
IEA
GO_REF:0000043
MODIFY
Summary: Correct but too general - SHMT catalyzes serine/glycine interconversion. A more specific child term, serine family amino acid biosynthetic process (GO:0009070), better captures the enzyme's role; the existing parent term should be kept as non-core.
Reason: The generic amino acid biosynthetic process term is uninformative for an SHMT; the serine family is the relevant subgroup and a more specific term is available.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
GlyA catalyzing the step that couples a folate-bound C1 unit with glycine to form serine
GO:0016740 transferase activity
IEA
GO_REF:0000043
KEEP AS NON CORE
Summary: Correct but too general - SHMT is a transferase, but the specific term "glycine hydroxymethyltransferase activity" (GO:0004372) is more informative and is already annotated.
GO:0019264 glycine biosynthetic process from L-serine
IEA
GO_REF:0000120
ACCEPT
Summary: Correct - SHMT catalyzes step 1/1 in glycine biosynthesis from L-serine. In the physiological methylotrophic direction in AM1 the reaction runs toward serine formation from glycine + an activated C1 unit, but the enzyme is fully reversible and this term is accurate.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
GlyA catalyzing the step that couples a folate-bound C1 unit with glycine to form serine
GO:0030170 pyridoxal phosphate binding
IEA
GO_REF:0000120
ACCEPT
Summary: Correct - SHMT is a PLP-dependent enzyme; PLP forms an internal aldimine (Schiff base) with the active-site lysine (Lys242 in this protein), confirmed by conserved SHMT structural studies.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
PLP forms an internal aldimine (Schiff base) with an active-site lysine
GO:0035999 tetrahydrofolate interconversion
IEA
GO_REF:0000120
ACCEPT
Summary: Correct - SHMT interconverts THF and 5,10-methylenetetrahydrofolate, the defining one-carbon transfer reaction of the serine cycle. In AM1 the physiologically relevant carrier is a polyglutamylated folate, which stimulates the SHMT reaction more strongly than monoglutamyl THF.
Supporting Evidence:
file:METEA/glyA/glyA-deep-research-falcon.md
polyglutamylated THF species stimulate SHMT-catalyzed serine synthesis more strongly than monoglutamyl THF in vitro
GO:0046653 tetrahydrofolate metabolic process
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: Correct but redundant - More specific term "tetrahydrofolate interconversion" (GO:0035999) captures the same process more precisely.
GO:0006545 glycine biosynthetic process
IEA
GO_REF:0000041
KEEP AS NON CORE
Summary: Correct - SHMT catalyzes glycine biosynthesis from serine; parent term of GO:0019264. Kept as non-core because the more specific GO:0019264 (glycine biosynthetic process from L-serine) is the precise term for this enzyme.

Core Functions

GlyA catalyzes the reversible, pyridoxal 5'-phosphate (PLP)-dependent interconversion of L-serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier, producing 5,10-methylenetetrahydrofolate. This enzyme is a central node of the serine cycle in methylotrophic metabolism, where it integrates C1 units from formaldehyde oxidation into cellular biosynthesis and is the first enzyme of the serine cycle. The reaction provides the major source of one-carbon units required for synthesis of purines, thymidylate, methionine, and other biomolecules. GlyA functions as a homodimer in the cytoplasm and is essential for methylotrophic growth: glyA null mutants lose all SHMT activity and cannot grow on C1 compounds (including methanol) even with glycine or serine supplementation, while growth on succinate is unaffected. The enzyme also exhibits THF-independent aldolase activity toward Ξ²-hydroxyamino acids via a retro-aldol mechanism.

Supporting Evidence:
  • file:METEA/glyA/glyA-uniprot.txt
    Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier...COFACTOR: Name=pyridoxal 5'-phosphate...Homodimer...Cytoplasm...Genetics of the serine cycle in Methylobacterium extorquens AM1
  • file:METEA/glyA/glyA-deep-research-falcon.md
    catalyzes the reversible folate-linked one-carbon transfer between serine and glycine: **L-serine + tetrahydrofolate (THF) ⇄ glycine + 5,10-methylenetetrahydrofolate (5,10-CH2-THF) + H2O**
  • file:METEA/glyA/glyA-deep-research-falcon.md
    GlyA is the **first enzyme of the serine cycle**
  • file:METEA/glyA/glyA-deep-research-falcon.md
    glyA mutants cannot grow on C1 compounds even when supplemented with glycine or serine

References

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