N-carbamoylputrescine amidohydrolase (EC 3.5.1.53), 292 aa, nitrilase /
carbon-nitrogen hydrolase superfamily (Pfam CN_hydrolase; NCBIfam TIGR03381
agmatine_aguB; InterPro IPR017755), with the Glu-Lys-Cys catalytic triad
(UniProt ACT_SITE 44, 117, 154). Second enzyme of the agmatine route from
arginine to putrescine (AguA agmatine deiminase, then AguB). Unreviewed
UniProt entry.
Other seeds' experimental support queried live in QuickGO on 2026-11-05.
| PTN node | node term | n_seeds | leaf IBAs | seed annotation (term, evidence, PMID) | verdict | rationale | other seeds | IBD stands without this seed? |
|---|---|---|---|---|---|---|---|---|
| PTN000557706 | GO:0050126 N-carbamoylputrescine amidase activity | 2 | 74 (57 taxa) | GO:0050126, IMP, PMID:6423933 (PseudoCAP) | SOUND | Abstract names aguB as the N-carbamoylputrescine amidohydrolase gene; the activity is independently confirmed with purified AguB (PMID:12634339). | Arabidopsis CPA/NLP1 AT2G27450 (Q8VYF5, IDA PMID:12435743) | Yes; the plant seed has IDA |
| PTN000557638 | GO:0016811 hydrolase activity, acting on C-N (but not peptide) bonds, in linear amides | 10 | 32 (23 taxa) | GO:0050126, IMP, PMID:6423933 (PseudoCAP) | SOUND | GO:0050126 is_a GO:0016811; broad node term suits a nitrilase-superfamily clade. | human, rat, mouse, worm, fly, Dictyostelium, Arabidopsis (x2), Helicobacter seeds | Yes; nine other seeds |
No PSEUDOCAP or GO_CENTRAL defect. The 1984 IMP is a genetics-led basis,
but the term is correct for the gene and is supported by later purified-enzyme
kinetics, so I do not ask for it to be changed. Adding an IDA from
PMID:12634339 would strengthen the seed; that is a curation suggestion, not a
defect.