ID:AMD_HUMAN DESCRIPTION: RecName: Full=Peptidyl-glycine alpha-amidating monooxygenase; Short=PAM; Includes: RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase; Short=PHM; EC=1.14.17.3; Includes: RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; EC=4.3.2.5; AltName: Full=Peptidylamidoglycolate lyase; Short=PAL; Flags: Precursor; FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity. CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide + glyoxylate. COFACTOR: Zinc; for the lyase reaction. COFACTOR: Binds 2 copper ions per subunit; For the monoxygenase reaction. ENZYME REGULATION: Inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate. SUBUNIT: Monomer. Interacts with RASSF9 (By similarity). SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Isoform 2: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Isoform 3: Secreted. Note=Secreted from secretory granules. SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Secreted from secretory granules. SIMILARITY: In the C-terminal section; belongs to the peptidyl- alpha-hydroxyglycine alpha-amidating lyase family. SIMILARITY: In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family. SIMILARITY: Contains 5 NHL repeats. SEQUENCE CAUTION: Sequence=AAD01439.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF01082 - Copper type II ascorbate-dependent monooxygenase, N-terminal domain PF01436 - NHL repeat PF03712 - Copper type II ascorbate-dependent monooxygenase, C-terminal domain
ModBase Predicted Comparative 3D Structure on P19021
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0003824 catalytic activity GO:0004497 monooxygenase activity GO:0004504 peptidylglycine monooxygenase activity GO:0004598 peptidylamidoglycolate lyase activity GO:0005507 copper ion binding GO:0005509 calcium ion binding GO:0005515 protein binding GO:0008270 zinc ion binding GO:0016491 oxidoreductase activity GO:0016715 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen GO:0016829 lyase activity GO:0019901 protein kinase binding GO:0031418 L-ascorbic acid binding GO:0046872 metal ion binding
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
