CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.620 | C8orf32 fold |
|
3.10.620.10 | Protein N-terminal glutamine amidohydrolase, alpha beta roll |
Domain Context
CATH Clusters
| Superfamily | Protein N-terminal glutamine amidohydrolase, alpha beta roll |
| Functional Family | Blast:Protein N-terminal glutamine amidohydrolase |
Enzyme Information
| 3.5.1.122 |
Protein N-terminal glutamine amidohydrolase.
based on mapping to UniProt Q96HA8
N-terminal L-glutaminyl-[protein] + H(2)O = N-terminal L-glutamyl- [protein] + NH(3).
-!- This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Gln. -!- Following the acetylation and removal of the initiator methionine, the exposed N-terminal glutamine is deaminated, resulting in its conversion to L-glutamate. -!- The latter serves as a substrate for EC 2.3.2.8 making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.
|
UniProtKB Entries (1)
| Q96HA8 |
NTAQ1_HUMAN
Homo sapiens
Protein N-terminal glutamine amidohydrolase
|
PDB Structure
| PDB | 3C9Q |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the uncharacterized human protein C8orf32 with bound peptide.
To be Published
|