cysH

Summary: CysH supplies sulfite for assimilatory reduced-sulfur biosynthesis.

Reason: The enzyme performs the APS-reduction step and thereby supplies reduced sulfur for cysteine synthesis; the native P. aeruginosa knockout is a cysteine auxotroph. This is catalytic pathway participation, not solely a downstream growth phenotype.

Summary: CysH supplies sulfite for assimilatory reduced-sulfur biosynthesis.

Reason: The enzyme performs the APS-reduction step and thereby supplies reduced sulfur for cysteine synthesis; the native P. aeruginosa knockout is a cysteine auxotroph. This is catalytic pathway participation, not solely a downstream growth phenotype.

Summary: CysH supplies sulfite for assimilatory reduced-sulfur biosynthesis.

Reason: The enzyme performs the APS-reduction step and thereby supplies reduced sulfur for cysteine synthesis; the native P. aeruginosa knockout is a cysteine auxotroph. This is catalytic pathway participation, not solely a downstream growth phenotype. PseudoCAP seed assessment (2026-11-05): this row is the PAO1 seed of the GO:0000103 IBD at PTN008207357. Verdict SOUND; the full text pairs the knockout with assays of the purified enzyme. The IBD also stands on the three Arabidopsis APR seeds, each with TAIR IDA rows for sulfate assimilation.

Summary: Refine catalytic activity to thioredoxin-dependent APS reduction.

Reason: The broad catalytic term is true; use the specific supported reaction.

Proposed replacements: adenylyl-sulfate reductase (thioredoxin) activity

Summary: The PAPS-reductase substrate assignment conflicts with the supported APS reaction.

Reason: Purified P. aeruginosa CysH reduces APS but not PAPS. APS-specific domain/cluster evidence supports this chemistry rather than transfer based on the broad PAPS/APS family name.

Summary: CysH is a cytoplasmic assimilatory enzyme.

Reason: Curated/HAMAP-supported localization places the soluble APS-reduction reaction in the cytoplasm; this is the location of its core activity.

Summary: Refine APS reductase activity to its thioredoxin-dependent reaction.

Reason: The enzyme reduces APS using thioredoxin; the existing more specific GO:0043866 captures the supported donor chemistry.

Proposed replacements: adenylyl-sulfate reductase (thioredoxin) activity

Summary: CysH supplies sulfite for assimilatory reduced-sulfur biosynthesis.

Reason: The enzyme performs the APS-reduction step and thereby supplies reduced sulfur for cysteine synthesis; the native P. aeruginosa knockout is a cysteine auxotroph. This is catalytic pathway participation, not solely a downstream growth phenotype.

Summary: CysH reduces APS with thioredoxin-derived reducing equivalents.

Reason: The purified P. aeruginosa reaction and thioredoxin adduct experiments establish the reaction. The [4Fe-4S] cluster accompanies APS specificity.

Summary: CysH reduces APS with thioredoxin-derived reducing equivalents.

Reason: The purified P. aeruginosa reaction and thioredoxin adduct experiments establish the reaction. The [4Fe-4S] cluster accompanies APS specificity.

Summary: CysH reduces APS with thioredoxin-derived reducing equivalents.

Reason: The purified P. aeruginosa reaction and thioredoxin adduct experiments establish the reaction. The [4Fe-4S] cluster accompanies APS specificity.

Summary: CysH reduces APS with thioredoxin-derived reducing equivalents.

Reason: The purified P. aeruginosa reaction and thioredoxin adduct experiments establish the reaction. The [4Fe-4S] cluster accompanies APS specificity.

Summary: The APS reductase carries a [4Fe-4S] cluster.

Reason: Mössbauer analysis directly identifies this cluster in P. aeruginosa CysH; conserved cluster ligands support the PAO1 inference.

Summary: CysH supplies sulfite for assimilatory reduced-sulfur biosynthesis.

Reason: The enzyme performs the APS-reduction step and thereby supplies reduced sulfur for cysteine synthesis; the native P. aeruginosa knockout is a cysteine auxotroph. This is catalytic pathway participation, not solely a downstream growth phenotype.