CysN is the GTPase subunit of the Escherichia coli CysDN ATP sulfurylase. Its GTP hydrolysis is energetically coupled to sulfate adenylation by CysD, producing APS for the sulfate-assimilation pathway. CysN therefore contributes to ATP sulfurylase activity through energy coupling rather than performing the sulfate adenyl-transfer reaction independently.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000103 sulfate assimilation | IDA PMID:2828368 The sulfate activation locus of Escherichia coli K12: clonin... | ACCEPT | Summary: CysN energetically couples sulfate activation to GTP hydrolysis. Reason: CysN is an active catalytic component of the sulfate activation machinery, not a consumed substrate. Its GTPase contribution enables the CysD reaction in sulfate assimilation. Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0000103 sulfate assimilation | IEA GO_REF:0000104 | ACCEPT | Summary: CysN energetically couples sulfate activation to GTP hydrolysis. Reason: CysN is an active catalytic component of the sulfate activation machinery, not a consumed substrate. Its GTPase contribution enables the CysD reaction in sulfate assimilation. Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0003924 GTPase activity | IDA PMID:1730615 GTPase-mediated activation of ATP sulfurylase. | ACCEPT | Summary: CysN is the GTPase component of ATP sulfurylase. Reason: Purified E. coli ATP sulfurylase hydrolyzes GTP, and the large CysN subunit contains the GTP-binding machinery. The 1994 coupling experiments establish the energetic relation to APS production. Supporting Evidence: PMID:1730615 The larger subunit of ATP sulfurylase, encoded by cysN, contains a GTP-binding consensus sequence common to other known GTP-binding proteins. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0003924 GTPase activity | IEA GO_REF:0000002 | ACCEPT | Summary: CysN is the GTPase component of ATP sulfurylase. Reason: Purified E. coli ATP sulfurylase hydrolyzes GTP, and the large CysN subunit contains the GTP-binding machinery. The 1994 coupling experiments establish the energetic relation to APS production. Supporting Evidence: PMID:1730615 The larger subunit of ATP sulfurylase, encoded by cysN, contains a GTP-binding consensus sequence common to other known GTP-binding proteins. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0004781 sulfate adenylyltransferase (ATP) activity | EXP PMID:8003495 The energetic linkage of GTP hydrolysis and the synthesis of... | ACCEPT | Summary: CysN contributes to sulfate adenylyltransferase activity in CysDN. Reason: Retain the established enzyme-level annotation: purified ATP sulfurylase requires both subunits. CysN hydrolyzes GTP while CysD adenylates sulfate; this does not mean isolated CysN performs the adenyl-transfer chemistry. The core function explicitly models a contribution to the complex reaction. Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0004781 sulfate adenylyltransferase (ATP) activity | IDA PMID:2828368 The sulfate activation locus of Escherichia coli K12: clonin... | ACCEPT | Summary: CysN contributes to sulfate adenylyltransferase activity in CysDN. Reason: Retain the established enzyme-level annotation: purified ATP sulfurylase requires both subunits. CysN hydrolyzes GTP while CysD adenylates sulfate; this does not mean isolated CysN performs the adenyl-transfer chemistry. The core function explicitly models a contribution to the complex reaction. Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0004781 sulfate adenylyltransferase (ATP) activity | IEA GO_REF:0000120 | ACCEPT | Summary: CysN contributes to sulfate adenylyltransferase activity in CysDN. Reason: Retain the established enzyme-level annotation: purified ATP sulfurylase requires both subunits. CysN hydrolyzes GTP while CysD adenylates sulfate; this does not mean isolated CysN performs the adenyl-transfer chemistry. The core function explicitly models a contribution to the complex reaction. Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: The reported physical association does not require a bare protein-binding function annotation. Reason: Apply the project's explicit GO:0005515 policy: bare protein binding is uninformative. This does not reject the interaction reported by PMID:24561554 or infer a wrong protein from incomplete source access. Specific catalytic contributions and complex membership are documented separately; an interaction-screen row alone does not identify an additional precise molecular function. |
| GO:0005515 protein binding | IPI PMID:2828368 The sulfate activation locus of Escherichia coli K12: clonin... | REMOVE | Summary: The reported physical association does not require a bare protein-binding function annotation. Reason: Apply the project's explicit GO:0005515 policy: bare protein binding is uninformative. This does not reject the interaction reported by PMID:2828368 or infer a wrong protein from incomplete source access. Specific catalytic contributions and complex membership are documented separately; an interaction-screen row alone does not identify an additional precise molecular function. |
| GO:0005525 GTP binding | IEA GO_REF:0000120 | ACCEPT | Summary: GTP binding is intrinsic to the CysN coupling reaction. Reason: The CysN GTP-binding consensus and nucleotide-dependent activation/turnover support substrate binding. Binding is a core feature of this metabolic GTPase. Supporting Evidence: PMID:1730615 The larger subunit of ATP sulfurylase, encoded by cysN, contains a GTP-binding consensus sequence common to other known GTP-binding proteins. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0005525 GTP binding | ISS PMID:1730615 GTPase-mediated activation of ATP sulfurylase. | ACCEPT | Summary: GTP binding is intrinsic to the CysN coupling reaction. Reason: The CysN GTP-binding consensus and nucleotide-dependent activation/turnover support substrate binding. Binding is a core feature of this metabolic GTPase. Supporting Evidence: PMID:1730615 The larger subunit of ATP sulfurylase, encoded by cysN, contains a GTP-binding consensus sequence common to other known GTP-binding proteins. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0006790 sulfur compound metabolic process | IBA GO_REF:0000033 | MODIFY | Summary: The specific sulfur pathway is sulfate assimilation. Reason: Refine this broad process to sulfate assimilation, already present here. The CysN GTPase supplies energy directly to the sulfate-activating step; this is not an assertion that CysN reduces sulfate itself. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN008591031 SUPPORTS TRANSFER The ancestral-node assertion is biologically compatible with this experimentally characterized target. Refinement specifies the supported process or catalytic reactions; it does not allege incorrect clade placement, inadequate donor count, or circularity from target self-inclusion. Proposed replacements: sulfate assimilation Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0006790 sulfur compound metabolic process | IEA GO_REF:0000002 | MODIFY | Summary: The specific sulfur pathway is sulfate assimilation. Reason: Refine this broad process to sulfate assimilation, already present here. The CysN GTPase supplies energy directly to the sulfate-activating step; this is not an assertion that CysN reduces sulfate itself. Proposed replacements: sulfate assimilation Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0006790 sulfur compound metabolic process | IMP PMID:2828368 The sulfate activation locus of Escherichia coli K12: clonin... | MODIFY | Summary: The specific sulfur pathway is sulfate assimilation. Reason: Refine this broad process to sulfate assimilation, already present here. The CysN GTPase supplies energy directly to the sulfate-activating step; this is not an assertion that CysN reduces sulfate itself. Proposed replacements: sulfate assimilation Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 |
| GO:0009336 sulfate adenylyltransferase complex (ATP) | IPI PMID:2828368 The sulfate activation locus of Escherichia coli K12: clonin... | ACCEPT | Summary: CysN is the large subunit of CysDN ATP sulfurylase. Reason: The original E. coli biochemical purification assigns the two subunits to cysD and cysN. Supporting Evidence: PMID:2828368 Purification of ATP sulfurylase to homogeneity reveals that the enzyme is composed of two types of subunits which are encoded by cysD and cysN. |
| GO:0070814 hydrogen sulfide biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: The enzyme participates in assimilatory hydrogen sulfide biosynthesis. Reason: cysN performs GTP-coupled sulfate activation, a direct catalytic contribution to the pathway producing sulfide from sulfate. This does not imply that every upstream enzyme itself releases sulfide or that the role is dissimilatory sulfur respiration. Supporting Evidence: PMID:8003495 The stoichiometry of GTP hydrolysis to APS synthesis is 1:1 file:ECOLI/cysN/cysN-uniprot.txt Sulfur metabolism; hydrogen sulfide biosynthesis; |
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