argC

UniProt ID: P11446
Organism: Escherichia coli K-12
Review Status: COMPLETE
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Gene Description

ArgC is the cytoplasmic type-1 N-acetyl-gamma-glutamyl-phosphate reductase of Escherichia coli. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate. This reaction supplies the carbon skeleton subsequently transaminated to N-acetylornithine during arginine biosynthesis.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase (NADP+) activity
IBA
GO_REF:0000033 		ACCEPT
Summary: The specific catalytic activity matches the independently supported reaction of this enzyme.
Reason: The specific catalytic activity matches the independently supported reaction of this enzyme. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase (NADP+) activity
IDA
PMID:13863980
N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semi... 		ACCEPT
Summary: The specific catalytic activity matches the independently supported reaction of this enzyme.
Reason: The specific catalytic activity matches the independently supported reaction of this enzyme. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase (NADP+) activity
IEA
GO_REF:0000120 		ACCEPT
Summary: The specific catalytic activity matches the independently supported reaction of this enzyme.
Reason: The specific catalytic activity matches the independently supported reaction of this enzyme. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0005737 cytoplasm
IEA
GO_REF:0000120 		ACCEPT
Summary: The soluble biosynthetic enzyme acts in the bacterial cytoplasm.
Reason: The soluble biosynthetic enzyme acts in the bacterial cytoplasm. Curated localization and the metabolic chemistry support this location; the cytosol assertion is compatible with a soluble enzyme rather than a membrane-bound catalyst.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00150}.
GO:0006526 L-arginine biosynthetic process
IBA
GO_REF:0000033 		ACCEPT
Summary: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly.
Reason: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP- Rule:MF_00150, ECO:0000305|PubMed:13863980}.
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0006526 L-arginine biosynthetic process
IDA
PMID:13863980
N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semi... 		ACCEPT
Summary: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly.
Reason: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP- Rule:MF_00150, ECO:0000305|PubMed:13863980}.
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0006526 L-arginine biosynthetic process
IDA
PMID:17651682
Continuous spectrophotometric assays for three regulatory en... 		ACCEPT
Summary: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly.
Reason: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP- Rule:MF_00150, ECO:0000305|PubMed:13863980}.
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0006526 L-arginine biosynthetic process
IEA
GO_REF:0000120 		ACCEPT
Summary: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly.
Reason: The enzyme directly catalyzes a step in this metabolic process rather than merely changing its outcome indirectly. It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP- Rule:MF_00150, ECO:0000305|PubMed:13863980}.
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
IEA
GO_REF:0000002 		MODIFY
Summary: The generic catalytic class is correct but the substrate-specific reaction is independently established.
Reason: The generic catalytic class is correct but the substrate-specific reaction is independently established. Refine to the supported molecular function already asserted in this review.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0051287 NAD binding
IEA
GO_REF:0000002 		MODIFY
Summary: GO:0051287 explicitly means NAD+/NADH binding.
Reason: GO:0051287 explicitly means NAD+/NADH binding. The supported ArgC reaction uses NADPH and produces NADP+, so refine the cofactor assignment to NADP+ binding. This is a correction to the supported phosphorylated cofactor, not a claim that an exhaustive NADH exclusion assay was performed.
Proposed replacements: NADP+ binding
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
GO:0070401 NADP+ binding
IEA
GO_REF:0000002 		ACCEPT
Summary: The reversible ArgC reaction directly uses the NADP+/NADPH pair, supporting binding of oxidized NADP+ as the product in the biosynthetic direction and substrate in the reverse direction.
Reason: The reversible ArgC reaction directly uses the NADP+/NADPH pair, supporting binding of oxidized NADP+ as the product in the biosynthetic direction and substrate in the reverse direction.
Supporting Evidence:
file:ECOLI/argC/argC-uniprot.txt
Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};

Core Functions

It uses NADPH to reduce N-acetylglutamyl phosphate to N-acetylglutamate semialdehyde, releasing phosphate.

Molecular Function:
N-acetyl-gamma-glutamyl-phosphate reductase (NADP+) activity
Directly Involved In:
L-arginine biosynthetic process
Cellular Locations:
cytoplasm
Supporting Evidence:
  • file:ECOLI/argC/argC-uniprot.txt
    Reaction=N-acetyl-L-glutamate 5-semialdehyde + phosphate + NADP(+) = N-acetyl-L-glutamyl 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:21588, ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38; Evidence={ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980};
  • file:ECOLI/argC/argC-uniprot.txt
    Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- L-ornithine from L-glutamate: step 3/4. {ECO:0000255|HAMAP- Rule:MF_00150, ECO:0000305|PubMed:13863980}.

References

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📚 Additional Documentation

Notes

(argC-notes.md)

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