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Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed. This subsection of the Names and taxonomy section shows the unique identifier assigned by the NCBI to the source organism of the protein. Cyclic redundancy and other checksums Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)) This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence. This subsection of the ‘Entry information’ section provides a mnemonic identifier for a Uni Prot KB entry, but it is not a stable identifier.

This is known as the ‘taxonomic identifier’ or ‘taxid’. This subsection of the Names and taxonomy section contains the taxonomic hierarchical classification lineage of the source organism. Each reviewed entry is assigned a unique entry name upon integration into Uni Prot KB/Swiss-Prot. This subsection of the ‘Entry information’ section provides one or more accession number(s).

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The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (Pub Med:12699694).

Peptidylglycine alpha-amidating monooxygenase (EC 1.14.17.3) is a multifunctional protein containing 2 enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), that act sequentially to catalyze the alpha-amidation of neuroendocrine peptides. Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21.



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