ArgC1 (PP_0432) is a type 1 N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38). It uses NADPH to reduce N-acetyl-L-glutamyl 5-phosphate to N-acetyl-L-glutamate 5-semialdehyde in the acetylated-ornithine route to L-arginine. KT2440 also encodes the type 2 isoenzyme ArgC2.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the defining ArgC1 molecular function. Reason: The reviewed UniProt record assigns EC 1.2.1.38, RHEA:21588, and the type 1 ArgC family to Q88QQ6. This assignment uses curated catalytic/family evidence; it is not a direct purified-enzyme measurement in KT2440. Supporting Evidence: file:PSEPK/argC1/argC1-uniprot.txt Catalyzes the NADPH-dependent reduction of N-acetyl-5- CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: The cytoplasm is the inferred compartment of this soluble biosynthetic enzyme. Reason: This location is part of the core metabolic role. It is supported by conserved soluble-enzyme biology and curated UniProt/HAMAP localization, not direct target imaging. Supporting Evidence: file:PSEPK/argC1/argC1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006526 L-arginine biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: The enzyme contributes catalytic chemistry to L-arginine biosynthesis. Reason: The enzyme catalyzes a chemical step of the acetylated-ornithine route to arginine, supported by curated reaction and family classification. Supporting Evidence: file:PSEPK/argC1/argC1-uniprot.txt Catalyzes the NADPH-dependent reduction of N-acetyl-5- CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. |
| GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor | IEA GO_REF:0000002 | MODIFY | Summary: Refine the true broad annotation to the supported substrate-specific function. Reason: The broad term is biologically compatible with the enzyme; the supported specific activity/process already present in this review is more informative. Breadth alone does not make a claim over-annotated. Proposed replacements: N-acetyl-gamma-glutamyl-phosphate reductase (NADP+) activity Supporting Evidence: file:PSEPK/argC1/argC1-uniprot.txt Catalyzes the NADPH-dependent reduction of N-acetyl-5- CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. |
| GO:0051287 NAD binding | IEA GO_REF:0000002 | MODIFY | Summary: The supported nicotinamide cofactor interaction is NADP(H). Reason: The broad NAD-domain mapping should be refined to NADP+ binding, supported by the target HAMAP chemistry and comparative M. tuberculosis structure. This is not evidence that the target cannot bind NAD or NADH; native cofactor selectivity has not been measured. Proposed replacements: NADP+ binding Supporting Evidence: file:PSEPK/argC1/argC1-uniprot.txt Catalyzes the NADPH-dependent reduction of N-acetyl-5- CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. PMID:17316682 the structure of MtbAGPR bound to the cofactor NADP(+) |
| GO:0070401 NADP+ binding | IEA GO_REF:0000002 | ACCEPT | Summary: NADP+ is the oxidized cofactor/product bound by the reductase. Reason: This is part of core redox chemistry; target curated HAMAP assignment is corroborated by comparative M. tuberculosis NADP-bound structure, not a direct KT2440 structural assay. Supporting Evidence: file:PSEPK/argC1/argC1-uniprot.txt Catalyzes the NADPH-dependent reduction of N-acetyl-5- CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. PMID:17316682 the structure of MtbAGPR bound to the cofactor NADP(+) |
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