CysNC is the GTPase-containing regulatory subunit 1 of the proteobacterial sulfate adenylyltransferase complex. It couples GTP hydrolysis to the CysD reaction that converts sulfate and ATP to APS. The protein also carries a C-terminal APS-kinase-like domain, but the catalytic contribution of that domain to the KT2440 complex remains unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000103 sulfate assimilation | IEA GO_REF:0000104 | ACCEPT | Summary: Correct pathway assignment for the regulatory ATP sulfurylase subunit. Reason: CysNC is required for energy-coupled APS formation in sulfate assimilation. |
| GO:0003924 GTPase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct subunit-specific molecular function. Reason: CysN-family regulatory subunits hydrolyze GTP to drive the otherwise unfavorable sulfate-adenylation reaction. Supporting Evidence: file:PSEPK/cysNC/cysNC-uniprot.txt GTP hydrolysis by CysN coupled |
| GO:0004781 sulfate adenylyltransferase (ATP) activity | IEA GO_REF:0000120 | MODIFY | Summary: Correct complex-level activity, but the imported enables qualifier incorrectly assigns the CysD-catalyzed reaction to CysNC itself. Reason: Q88NA8 is required in the physiological ATP sulfurylase complex, but its subunit-specific catalytic activity is GTP hydrolysis. Retain GO:0004781 with contributes_to rather than enables. Proposed replacements: sulfate adenylyltransferase (ATP) activity Supporting Evidence: file:PSEPK/cysNC/cysNC-uniprot.txt With CysD forms the ATP sulfurylase (ATPS) that catalyzes the |
| GO:0005525 GTP binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Correct supporting nucleotide-binding property. Reason: GTPase activity captures the functional consequence of GTP binding. |
| GO:0006790 sulfur compound metabolic process | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Correct but excessively broad process parent. Reason: GO:0000103 identifies the relevant sulfate-assimilation process. |
| GO:0070814 hydrogen sulfide biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: Correct downstream process assignment. Reason: CysNC-dependent APS formation initiates the sulfate-to-sulfide route. |
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Download this section (compressed HTML)Q: Is the C-terminal APS-kinase-like domain of Q88NA8 catalytically active, or is it a retained but inactive fusion remnant in the direct APS-reduction route?
Experiment: Reconstitute Q88NA8/Q88NA9 and quantify both APS and PAPS formation, then test isolated C-terminal-domain and active-site variants for APS kinase activity.
Type: pathway reconstitution and domain-function assay
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