carA encodes the glutaminase small chain of carbamoyl-phosphate synthase. It hydrolyzes glutamine and channels ammonia to CarB for ATP-dependent carbamoyl-phosphate formation serving both de novo UMP and L-arginine biosynthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | IEA GO_REF:0000120 | REMOVE | Summary: CarA supplies the glutaminase component of the two-chain glutamine-dependent carbamoyl-phosphate synthase. Reason: The enables relation is incorrect because CarA contributes its glutaminase reaction to the overall two-chain activity; it does not catalyze the complete glutamine-dependent synthesis reaction alone. A separate contributes_to row captures the supported relation. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt Small subunit of the glutamine-dependent carbamoyl phosphate |
| GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | ISS file:PSEPK/carA/carA-uniprot.txt | NEW | Summary: CarA contributes the glutaminase component of the two-chain CarAB activity. Reason: CarA hydrolyzes glutamine and supplies ammonia to CarB, so its relationship to the complete glutamine-dependent synthase activity is contributes_to. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt Small subunit of the glutamine-dependent carbamoyl phosphate |
| GO:0004359 glutaminase activity | IEA GO_REF:0000116 | ACCEPT | Summary: CarA hydrolyzes glutamine to glutamate and ammonium. Reason: Rhea 15889 in the reviewed record directly defines this small-chain reaction. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt Reaction=L-glutamine + H2O = L-glutamate + NH4(+); file:PSEPK/carA/carA-deep-research-openscientist.md of *Pseudomonas putida* KT2440 encodes the **small glutaminase subunit of carbamoyl phosphate synthetase (EC 6.3.5.5)** |
| GO:0005524 ATP binding | IEA GO_REF:0000104 | REMOVE | Summary: ATP is consumed by the CarB large chain, not by the CarA glutaminase chain. Reason: CarA contains the glutaminase domain and its assigned component reaction is ATP-independent; this electronic transfer conflates the two subunits. Supporting Evidence: file:PSEPK/carB/carB-uniprot.txt The large subunit is composed of 2 ATP-grasp domains that are |
| GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: CarA contributes carbamoyl phosphate to de novo pyrimidine synthesis. Reason: The more specific de novo UMP biosynthetic process is present and preferred. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; |
| GO:0006526 L-arginine biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: The shared CarAB carbamoyl-phosphate synthase supplies the arginine pathway. Reason: The reviewed record explicitly assigns the arginine biosynthesis branch. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl |
| GO:0006541 L-glutamine metabolic process | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: CarA directly hydrolyzes glutamine, but this broad process does not capture the biosynthetic purpose of the reaction. Reason: Glutamine is a substrate of the reaction, but this broad process obscures the biosynthetic roles in UMP and arginine production. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt Reaction=L-glutamine + H2O = L-glutamate + NH4(+); |
| GO:0044205 'de novo' UMP biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: CarA contributes the first reaction of de novo UMP biosynthesis. Reason: The reviewed record explicitly assigns this pathway branch. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; |
| GO:0005951 carbamoyl-phosphate synthase complex | ISS file:PSEPK/carA/carA-uniprot.txt | NEW | Summary: CarA is the glutaminase chain of the two-chain carbamoyl-phosphate synthase complex. Reason: The reviewed record explicitly describes the enzyme as a two-chain complex. Supporting Evidence: file:PSEPK/carA/carA-uniprot.txt Composed of two chains; the small (or glutamine) chain |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: How tightly is ammonia transfer from CarA coupled to the two ATP-dependent partial reactions on CarB in the KT2440 heterodimer?
Experiment: Co-express KT2440 CarA and CarB, compare glutamine-dependent and ammonia-dependent carbamoyl-phosphate synthesis, and test a CarA Cys269 substitution to verify glutaminase coupling and ammonia channeling.
Type: biochemical reconstitution assay
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)