Function
Forms APS as the activated sulfate intermediate.
A reusable pathway that converts sulfate to sulfide through adenosine 5'-phosphosulfate (APS) and sulfite. The module contains sulfate activation by ATP sulfurylase, thioredoxin-dependent APS reduction, and assimilatory sulfite reduction. It represents the direct APS branch rather than the alternative APS-kinase/PAPS-reductase route. Sulfate import is upstream, whereas siroheme synthesis and incorporation of sulfide into cysteine are supporting or downstream biology outside the pathway boundary.
All recommended fields populated.
✗ none found
No MODULE:aps_dependent_assimilatory_sulfate_reduction deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
4 complete review(s) · 2 with deep research · 5 missing review · 3 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| cysD Q88NA9 | ✓ | ✓ | ✗ |
| cysH Q88KG2 | ✓ | ✓ | ✓ |
| cysI Q88KB9 | ✓ | ✓ | ✓ |
| cysNC Q88NA8 | ✓ | ✓ | ✗ |
| fpr-I Q88MD5 | ✓ | 3/5 | ✗ |
| Escherichia coli K-12 CysI P17846 | ✗ | — | — |
| Escherichia coli K-12 CysD P21156 | ✗ | — | — |
| Escherichia coli K-12 CysN P23845 | ✗ | — | — |
| Escherichia coli K-12 CysJ P38038 | ✗ | — | — |
| Mycobacterium tuberculosis Sir P9WJ02 | ✗ | — | — |
This module deliberately represents the direct APS-reduction route. An APS-kinase/PAPS-reductase branch should be modeled as a separate route variant rather than adding a PAPS step to every instance. Exact UniProt exemplars delimit the CysD/CysN, ferredoxin/Fpr, and CysJ/CysI implementations without restricting the module taxonomically. No molecular function or location is duplicated at module level, and no ancestral PTN node is asserted without verified PAINT IBD evidence.
Forms APS as the activated sulfate intermediate.
Reduces APS directly to sulfite without a PAPS intermediate.
The catalytic siroheme/iron-sulfur hemoprotein is conserved, but lineages differ in whether electrons arrive through a separate CysJ flavoprotein or a ferredoxin/Fpr system.
A CysI-family sulfite reductase receives reducing equivalents from reduced ferredoxin or directly from a type-1 Fpr enzyme. This architecture occurs in bacterial systems that lack the classical CysJ diflavin partner.
Performs the six-electron reduction of sulfite.
Supplies reducing equivalents to the CysI system through ferredoxin or direct electron transfer.
The classical enterobacterial implementation uses a CysJ diflavin subunit to transfer electrons from NADPH to the CysI siroheme/iron-sulfur catalytic subunit.
Performs NADPH-dependent reduction of sulfite to sulfide.