hyuC (PP_4034) encodes a zinc-dependent M20-family amidohydrolase near the reductive pyrimidine-catabolic locus. Its physiological substrate is unresolved: beta-ureidopropionase would complete that pathway, whereas its PANTHER/InterPro assignments support allantoate or N-carbamoyl-L-amino-acid hydrolysis as alternatives. PP_0614 is a second KT2440 protein carrying the same dual beta-ureidopropionase/allantoate submitter annotation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003837 beta-ureidopropionase activity | IEA GO_REF:0000003 | UNDECIDED | Summary: Beta-ureidopropionase is a plausible pathway-completion hypothesis, but the annotation is not independently supported. Reason: This EC-derived IEA and the submitted protein name trace to the same 2002 EMBL annotation, so the name cannot independently validate the GO term. PTHR32494:SF5 favors an allantoate-family assignment, related hyuC exemplars hydrolyze N-carbamoyl-L-amino acids, and PP_0614 is an alternative KT2440 candidate for the terminal pyrimidine-catabolic step. |
| GO:0016787 hydrolase activity | IEA GO_REF:0000002 | ACCEPT | Summary: HyuC is a metal-dependent hydrolase, although this generic activity does not identify its physiological substrate. Reason: This is the only seeded catalytic term that remains valid across the competing substrate assignments. |
| GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines | IEA GO_REF:0000002 | UNDECIDED | Summary: This EC 3.5.3.- reaction class supports the allantoate/amidine branch and is not a parent of beta-ureidopropionase. Reason: InterPro IPR010158 supports an amidine-hydrolase family assignment, but accepting it would prejudge the unresolved target substrate. The alternative beta-ureidopropionase reaction belongs under the linear-amide branch GO:0016811. |
| GO:0047652 allantoate deiminase activity | IEA GO_REF:0000003 | UNDECIDED | Summary: The EC-derived allantoate assignment agrees with PTHR32494:SF5 and GO:0016813, but no KT2440 substrate-specific assay was found. Reason: The same record is mapped to beta-ureidopropionase and allantoate deiminase from one submitter annotation. Family evidence favors this branch but does not establish Q88FQ3 substrate turnover, so the activity cannot yet be accepted or removed. |
| GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | IC file:PSEPK/hyuC/hyuC-notes.md | NEW | Summary: The competing beta-ureidopropionase, allantoate, and carbamoyl-amino-acid assignments all imply nonpeptide C-N bond hydrolysis. Reason: This common reaction-class ancestor captures the supported catalytic chemistry without selecting an unverified physiological substrate. Supporting Evidence: file:PSEPK/hyuC/hyuC-uniprot.txt DR InterPro; IPR010158; Amidase_Cbmase. |
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