ASP5

Summary: Use the directly demonstrated aminotransferase activities.

Reason: General catalysis/transamination is correct but less informative than the supported specific reactions.

Proposed replacements: L-aspartate:2-oxoglutarate transaminase activity

Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination.

Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence.

Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination.

Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence.

Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination.

Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence.

Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination.

Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence.

Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination.

Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence.

Summary: The enzyme catalyzes aspartate/2-oxoglutarate transamination.

Reason: Direct target enzymology supports reversible Asp/Glu interconversion. PMID:9535706 measures all four substrates for recombinant ASP2 and ASP5; PMID:12068109 provides native isozyme-mutant evidence.

Summary: The ASP5 localization exclusion remains unresolved.

Reason: The seeded annotation explicitly excludes cytosolic localization. Plastid/chloroplast targeting of ASP5 supports its principal organellar location, but does not alone establish absence of a minor or conditional cytosolic pool. The precise target-specific exclusion behind the PMID:21166475 proteomic classification could not be resolved from accessible material.

Summary: Plasma membrane assignment needs target-specific resolution.

Reason: PMID:28887381 Supplement S1 lists the ASP5 isoform group as plastid with a membrane-protein flag. That flag does not specifically demonstrate plasma membrane localization.

Summary: The transaminase directly metabolizes this reaction substrate/product.

Reason: The measured reversible reaction interconverts aspartate, glutamate, oxaloacetate and 2-oxoglutarate. Native evidence in PMID:12068109 supports physiological Asp-family metabolism without requiring every mutant to be a complete null.

Summary: Specify the experimentally grounded amino-acid processes.

Reason: For ASP2/ASP5 the reversible AspAT reaction directly metabolizes Asp and Glu. PAT additionally catalyzes arogenate formation in phenylalanine biosynthesis; broad precursor supply alone does not establish every downstream pathway.

Proposed replacements: aspartate metabolic process glutamate metabolic process

Summary: The transaminase directly metabolizes this reaction substrate/product.

Reason: The measured reversible reaction interconverts aspartate, glutamate, oxaloacetate and 2-oxoglutarate. Native evidence in PMID:12068109 supports physiological Asp-family metabolism without requiring every mutant to be a complete null.

Summary: The transaminase directly metabolizes this reaction substrate/product.

Reason: The measured reversible reaction interconverts aspartate, glutamate, oxaloacetate and 2-oxoglutarate. Native evidence in PMID:12068109 supports physiological Asp-family metabolism without requiring every mutant to be a complete null.

Summary: Use the directly demonstrated aminotransferase activities.

Reason: General catalysis/transamination is correct but less informative than the supported specific reactions.

Proposed replacements: L-aspartate:2-oxoglutarate transaminase activity

Summary: ASP5 abundance responds to cold acclimation.

Reason: Retain the curator-linked protein-abundance response in PMID:16923014 as a contextual response, not evidence for a dedicated cold-sensing mechanism; plastid metabolic remodeling is compatible with its established enzyme role.

Summary: Retain amyloplast localization as a qualified plastid-subtype assignment.

Reason: PMID:9535706 explicitly suggested the amyloplastic rather than chloroplastic identity from native/recombinant isozyme comparison; this is a qualified interpretation, not direct organelle imaging. Later chloroplast evidence does not exclude non-green plastids.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 chloroplast import/native isozyme assignment and PAT curated plastid targeting support the compartment; stroma rows are retained as consistent subplastid proteomic evidence from PMID:20061580, without interpreting stroma as stromule. Older study PMID:9535706 amyloplast suggestion is not an exclusion of chloroplast residence. The import assay uses Arabidopsis precursor and isolated pea chloroplasts; native Arabidopsis activity assignment in PMID:12068109 is separate evidence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: The enzyme acts in plastids, with chloroplast evidence.

Reason: ASP5 is curated as chloroplast-localized in its own UniProt record. ASP5 precursor import into isolated pea chloroplasts (PMID:7766905) and native Arabidopsis isozyme/mutant assignment (PMID:12068109) provide convergent compartment evidence. The chloroplast-stroma annotation is retained as convergent curator-reviewed subplastid proteomic evidence; this does not establish stromule residence.

Summary: Chloroplast envelope assignment needs target-specific resolution.

Reason: Envelope fraction detection in PMID:12938931 is compatible with import or peripheral association, but stable ASP5 envelope residency versus stromal carryover was not independently resolved.

Summary: Stromule assignment needs target-specific resolution.

Reason: PMID:16923014 examines stromal and lumen proteomes; the target-specific evidence for a stromule was not accessible. Stroma and stromule are distinct, so neither substitution nor rejection is made from the title.

Summary: Pyridoxal phosphate is the integral catalytic cofactor.

Reason: The conserved PLP-dependent aminotransferase mechanism and curated cofactor information support this core binding property.

Summary: Retain the experimentally supported absence of prephenate transfer by ASP5.

Reason: Full text of PMID:20883697 Methods 2.6 tests recombinant At4g31990 separately from PAT At2g22250. Results 3.2 reports active AspAT but no detectable PAT activity at 1 mM prephenate. This is a bounded substrate-specific negative, not an absence inferred from another paralog.

Summary: Retain the experimentally supported absence of prephenate transfer by ASP5.

Reason: Full text of PMID:20883697 Methods 2.6 tests recombinant At4g31990 separately from PAT At2g22250. Results 3.2 reports active AspAT but no detectable PAT activity at 1 mM prephenate. This is a bounded substrate-specific negative, not an absence inferred from another paralog.

Summary: Apoplast assignment needs target-specific resolution.

Reason: PMID:18538804 uses whole-plant isotope labeling and oxidative-stress proteomics. The exact apoplastic target evidence was not recovered; plastid localization does not by itself disprove another pool.