APS1 (At3g22890), also called ATPS1, is a plastid ATP sulfurylase that activates sulfate with ATP to form APS and pyrophosphate. Its abundance contributes to control of sulfate assimilation and leaf sulfate pools. APS1 also supports selenate assimilation when expressed in transgenic plants. It is a monofunctional sulfurylase, distinct from the plant APS kinases that phosphorylate APS to PAPS.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000103 sulfate assimilation | IBA GO_REF:0000033 | ACCEPT | Summary: APS1 catalyzes sulfate activation upstream of reduced-sulfur biosynthesis. Reason: APS1 performs the first enzymatic step of sulfate assimilation; native disruption lowers sulfurylase activity and sulfate flux. Downstream sulfide production includes this activation step. Supporting Evidence: PMID:8058839 Expression of APS1 correlated with the presence of ATP sulfurylase enzyme activity in cell extracts. PMID:24027241 Disruption of the ATPS1 gene in Col-0 resulted in the reduction of ATPS enzyme activity by approximately 50% |
| GO:0000103 sulfate assimilation | IEA GO_REF:0000002 | ACCEPT | Summary: APS1 catalyzes sulfate activation upstream of reduced-sulfur biosynthesis. Reason: APS1 performs the first enzymatic step of sulfate assimilation; native disruption lowers sulfurylase activity and sulfate flux. Downstream sulfide production includes this activation step. Supporting Evidence: PMID:8058839 Expression of APS1 correlated with the presence of ATP sulfurylase enzyme activity in cell extracts. PMID:24027241 Disruption of the ATPS1 gene in Col-0 resulted in the reduction of ATPS enzyme activity by approximately 50% |
| GO:0001887 selenium compound metabolic process | IMP PMID:15941393 Analysis of sulfur and selenium assimilation in Astragalus p... | KEEP AS NON CORE | Summary: APS1 supports selenium assimilation in transgenic plant experiments. Reason: The original Astragalus paper also assays transgenic Arabidopsis; its title is not a reason to reject the annotation. Independent PMID:9880353 specifically expresses Arabidopsis APS1 in Indian mustard and observes enhanced selenate reduction. This supports a peripheral substrate capability, without confusing ATP-dependent activation with reductase catalysis. Supporting Evidence: PMID:9880353 the Arabidopsis APS1 gene, encoding a plastidic ATP sulfurylase, was constitutively overexpressed in Indian mustard PMID:9880353 The APS plants showed increased selenate reduction |
| GO:0004020 adenylylsulfate kinase activity | IBA GO_REF:0000033 | REMOVE | Summary: APS1 is a monofunctional ATP sulfurylase, not an APS kinase. Reason: The existing family review scopes kinase activity away from SF46 and flags PTN000114732 for pruning on plant sulfurylases. APS1 has sulfurylase/PUA architecture without the kinase domain, and target complementation/activity establishes sulfate adenylation. The challenge is to ancestral-node propagation across distinct domain architectures, not to the number or identity of donor annotations. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000114732 · APS kinase ancestral assertion SUPPORTS SOURCE BUT NOT TARGET Existing PTHR11055 family review flags this node for pruning on SF46/SF37/SF77/SF39 plant ATP sulfurylases; the donor enzymes have APS-kinase domains, APS1 does not. Supporting Evidence: PMID:8058839 Expression of APS1 correlated with the presence of ATP sulfurylase enzyme activity in cell extracts. file:ARATH/APS1/APS1-uniprot.txt Pfam; PF01747; ATP-sulfurylase; 1. file:ARATH/APS1/APS1-uniprot.txt Pfam; PF14306; PUA_2; 1. |
| GO:0004781 sulfate adenylyltransferase (ATP) activity | IEA GO_REF:0000120 | ACCEPT | Summary: APS1 catalyzes ATP-dependent sulfate adenylation. Reason: Target APS1 complementation and enzyme activity establish the reaction. PMID:7487067 purified recombinant APS3 for detailed kinetics; those kinetic values are not assigned to APS1. Native APS1 perturbation independently supports sulfurylase activity. Supporting Evidence: PMID:8058839 Expression of APS1 correlated with the presence of ATP sulfurylase enzyme activity in cell extracts. PMID:24027241 Disruption of the ATPS1 gene in Col-0 resulted in the reduction of ATPS enzyme activity by approximately 50% |
| GO:0004781 sulfate adenylyltransferase (ATP) activity | TAS PMID:7487067 Adenosine-5'-triphosphate-sulfurylase from Arabidopsis thali... | ACCEPT | Summary: APS1 catalyzes ATP-dependent sulfate adenylation. Reason: Target APS1 complementation and enzyme activity establish the reaction. PMID:7487067 purified recombinant APS3 for detailed kinetics; those kinetic values are not assigned to APS1. Native APS1 perturbation independently supports sulfurylase activity. Supporting Evidence: PMID:8058839 Expression of APS1 correlated with the presence of ATP sulfurylase enzyme activity in cell extracts. PMID:24027241 Disruption of the ATPS1 gene in Col-0 resulted in the reduction of ATPS enzyme activity by approximately 50% |
| GO:0005829 cytosol | RCA NOT PMID:21166475 Analysis of the Arabidopsis cytosolic proteome highlights su... | ACCEPT | Summary: APS1 is not a cytosolic protein; the NOT-cytosol assertion is independently confirmed by in vivo GFP localization. Reason: The curator assigned NOT cytosol to APS1 from the cytosolic-proteome study (PMID:21166475), which defines a set of proteins not targeted to organelles. An independent target-specific test settles the question that the abstract-only cache left open. Bohrer et al. (PMID:25601874) fused the native ATPS1 5' UTR and N-terminal region to GFP in protoplasts and expressed ATPS1pro:ATPS1-GFP in stable lines. ATPS1-GFP was exclusively plastidic, whereas ATPS2, through alternative translational initiation, was dually localized in plastids and cytosol. The cytosolic ATP sulfurylase pool in Arabidopsis therefore comes from ATPS2, not APS1, and the negative claim holds. Supporting Evidence: PMID:25601874 In contrast, the transfection of ATPS1(5′UTR−Val63)-GFP showed exclusive localization of GFP in the chloroplasts (Figure 3C). PMID:25601874 At subcellular levels, signals of GFP were dually localized in plastids and cytosol in both leaves and roots of ATPS2-GFP lines (Figure 4C), while they were present only in plastids in ATPS1-GFP lines (Figure 4D). |
| GO:0009507 chloroplast | HDA PMID:18431481 Sorting signals, N-terminal modifications and abundance of t... | MODIFY | Summary: Refine chloroplast localization to chloroplast stroma. Reason: Target import and independent curated stromal localization support the existing more specific stromal term. The general plastid-location claim is true, not an over-annotation. Proposed replacements: chloroplast stroma Supporting Evidence: PMID:8058839 the APS1 polypeptide, synthesized in vitro, is capable of entering isolated intact chloroplasts. file:ARATH/APS1/APS1-uniprot.txt Plastid, chloroplast stroma |
| GO:0009507 chloroplast | IDA PMID:8058839 Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis ... | MODIFY | Summary: Refine chloroplast localization to chloroplast stroma. Reason: Target import and independent curated stromal localization support the existing more specific stromal term. The general plastid-location claim is true, not an over-annotation. Proposed replacements: chloroplast stroma Supporting Evidence: PMID:8058839 the APS1 polypeptide, synthesized in vitro, is capable of entering isolated intact chloroplasts. file:ARATH/APS1/APS1-uniprot.txt Plastid, chloroplast stroma |
| GO:0009507 chloroplast | ISM GO_REF:0000122 | MODIFY | Summary: Refine chloroplast localization to chloroplast stroma. Reason: Target import and independent curated stromal localization support the existing more specific stromal term. The general plastid-location claim is true, not an over-annotation. Proposed replacements: chloroplast stroma Supporting Evidence: PMID:8058839 the APS1 polypeptide, synthesized in vitro, is capable of entering isolated intact chloroplasts. file:ARATH/APS1/APS1-uniprot.txt Plastid, chloroplast stroma |
| GO:0009570 chloroplast stroma | HDA PMID:16207701 The oligomeric stromal proteome of Arabidopsis thaliana chlo... | ACCEPT | Summary: APS1 acts in chloroplast stroma. Reason: Independent target import plus the curated stromal assignment and repeated chloroplast-proteomic evidence support the location. A limited individual abstract does not negate the independently established claim. Supporting Evidence: PMID:8058839 the APS1 polypeptide, synthesized in vitro, is capable of entering isolated intact chloroplasts. file:ARATH/APS1/APS1-uniprot.txt Plastid, chloroplast stroma |
| GO:0009570 chloroplast stroma | HDA PMID:18633119 Quantitative proteomics of a chloroplast SRP54 sorting mutan... | ACCEPT | Summary: APS1 acts in chloroplast stroma. Reason: Independent target import plus the curated stromal assignment and repeated chloroplast-proteomic evidence support the location. A limited individual abstract does not negate the independently established claim. Supporting Evidence: PMID:8058839 the APS1 polypeptide, synthesized in vitro, is capable of entering isolated intact chloroplasts. file:ARATH/APS1/APS1-uniprot.txt Plastid, chloroplast stroma |
| GO:0009570 chloroplast stroma | HDA PMID:20061580 AT_CHLORO, a comprehensive chloroplast proteome database wit... | ACCEPT | Summary: APS1 acts in chloroplast stroma. Reason: Independent target import plus the curated stromal assignment and repeated chloroplast-proteomic evidence support the location. A limited individual abstract does not negate the independently established claim. Supporting Evidence: PMID:8058839 the APS1 polypeptide, synthesized in vitro, is capable of entering isolated intact chloroplasts. file:ARATH/APS1/APS1-uniprot.txt Plastid, chloroplast stroma |
| GO:0009570 chloroplast stroma | IEA GO_REF:0000044 | ACCEPT | Summary: APS1 acts in chloroplast stroma. Reason: Independent target import plus the curated stromal assignment and repeated chloroplast-proteomic evidence support the location. A limited individual abstract does not negate the independently established claim. Supporting Evidence: PMID:8058839 the APS1 polypeptide, synthesized in vitro, is capable of entering isolated intact chloroplasts. file:ARATH/APS1/APS1-uniprot.txt Plastid, chloroplast stroma |
| GO:0046686 response to cadmium ion | IEP PMID:17075075 Proteome changes in Arabidopsis thaliana roots upon exposure... | KEEP AS NON CORE | Summary: ATP sulfurylase abundance responds to cadmium exposure in roots. Reason: The native root-proteome experiment identifies ATP sulfurylase among proteins with altered abundance after cadmium treatment. Retain the curator’s APS1 assignment as a contextual response; this does not assign cadmium binding or detoxification catalysis to APS1. Supporting Evidence: PMID:17075075 Most of the identified proteins belong to four different classes: metabolic enzymes such as ATP sulphurylase |
| GO:0070814 hydrogen sulfide biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: APS1 catalyzes sulfate activation upstream of reduced-sulfur biosynthesis. Reason: APS1 performs the first enzymatic step of sulfate assimilation; native disruption lowers sulfurylase activity and sulfate flux. Downstream sulfide production includes this activation step. Supporting Evidence: PMID:8058839 Expression of APS1 correlated with the presence of ATP sulfurylase enzyme activity in cell extracts. PMID:24027241 Disruption of the ATPS1 gene in Col-0 resulted in the reduction of ATPS enzyme activity by approximately 50% |
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