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A0A852MZB7 · A0A852MZB7_9PASS

  • Protein
    AMD monooxygenase
  • Gene
    Pam
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 2 Cu2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds one Zn2+ ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site103Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site104Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site168Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site238Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site240Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site310Cu2+ 1 (UniProtKB | ChEBI); catalytic
Binding site514Ca2+ (UniProtKB | ChEBI); structural
Binding site527C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site579Zn2+ (UniProtKB | ChEBI); catalytic
Binding site581Ca2+ (UniProtKB | ChEBI); structural
Binding site647C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site683Zn2+ (UniProtKB | ChEBI); catalytic
Binding site699C-terminal Xaa-(2S)-2-hydroxyglycine residue (UniProtKB | ChEBI) of a protein (UniProtKB | ChEBI)
Binding site780Zn2+ (UniProtKB | ChEBI); catalytic
Binding site781Ca2+ (UniProtKB | ChEBI); structural

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenttransport vesicle membrane
Molecular Functioncopper ion binding
Molecular Functionlyase activity
Molecular Functionpeptidylglycine monooxygenase activity
Biological Processpeptide metabolic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • AMD monooxygenase

Gene names

    • Name
      Pam
    • ORF names
      PTEMEL_R08634

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B10K-IZ-033-77
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Sylvioidea > Timaliidae > Pteruthius

Accessions

  • Primary accession
    A0A852MZB7

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane860-884Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-21
ChainPRO_503276766422-984
Disulfide bond43↔182
Disulfide bond77↔122
Disulfide bond110↔127
Disulfide bond223↔330
Disulfide bond289↔311
Disulfide bond627↔648
Disulfide bond695↔706
Glycosylation759N-linked (GlcNAc...) asparagine

Keywords

Family & Domains

Features

Showing features for domain, repeat, region.

Type
IDPosition(s)Description
Domain61-172Copper type II ascorbate-dependent monooxygenase N-terminal
Domain197-342Copper type II ascorbate-dependent monooxygenase C-terminal
Repeat567-605NHL
Repeat613-658NHL
Repeat676-710NHL
Region948-984Disordered

Sequence similarities

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.
In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    984
  • Mass (Da)
    110,184
  • Last updated
    2021-09-29 v1
  • MD5 Checksum
    FFFD351D999BC50A3791870F12ACFB0B
MAGFVNNLLILLLLFQNICLGFRSPLSVFKRYKDTTRSLSSECLGSDQPVVSFGLSDFALDIRMPGVTPKQSDTYLCMSVPLPVDCEAYVVDFKPHASMDTVHHMLVFGCNEPSSTENYWDCDQGTCKDKSNILYAWARNAPPTRLPKGVGFRVGGETGSRYFVLQVHYGDVSAFRDKHKDCSGVTLHLTHQKQPLIAGMYLMMSVNTVIPPGEKVVNADIACHYKRSPMHLFAYRVHTHRLGKLVSGYRVRNGQWTLIGRQSPQLPQAFYPVEYPVDISYNDILAARCVFSGEGRTTETHIGGTANDEMCNFYIMYYMEAKHAVSYMTCTQNANPEMFRNIPQEANIPIPVKSDVLKMMHGHHEETKDSDTNSLLQQAKKEEKEIWDQGGFYSLLSKLLGEREDVVHVHKQNPTEKSEPDLVAEIADVVQKKDLAREIANHDERDHTILVRDRIQKFHRLESTLRPPENRHFSLQQPKLGEGSWEKEHKRDFHIEEAVEWPGLDLKLGQVSGLALDPENNLIVFHRGDRVWDENSFDSKFVYQQRGLGPIEQNTILVLNPSNAKLLHSTGKSLFYLPHGLSVDKNGNYWVTDVALHQVFKLGGNDKEPLLILGVALQPGSDKNHFCQPTDVAVDPVTGSIYVSDGYCNSRIIQFSPNGLYVMQWGEETSLGRARPGQFHIPHSLALIPDLSQLCVADRENGRIQCFRLETGEFTREIKHKAFGRELFAVSYVPGGLLFAVNGMPYPGEAESVQGFVMNFSTGEIIDTFIPLRKSFEMPHDIVASEDRTVFVGDVHAKAVWKFASAEKMEHRSVKKAGIEVQETKESETIVEARLKNKPESTDPLKKTDKHLVQQASSTGVSFVLITTLLTIPVVVLLAILVFIRWRKTTLYGADGEHKLGSSPGRILGRLRGNKPYENPFLSTGKGGGGINLGNFFASHKGYSRKGFDRLSTEGSDQEKDEDDGTDSEEECSASPLPPAPLSS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue984

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WEIY01000300
EMBL· GenBank· DDBJ
NXY06128.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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