Pam peptidylglycine alpha-amidating monooxygenase [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Pamprovided by MGI
Official Full Name: peptidylglycine alpha-amidating monooxygenaseprovided by MGI
Primary source: MGI:MGI:97475
See related: Ensembl:ENSMUSG00000026335 AllianceGenome:MGI:97475
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: PHM
Summary: Predicted to enable several functions, including metal ion binding activity; peptidylamidoglycolate lyase activity; and peptidylglycine monooxygenase activity. Predicted to be involved in several processes, including fatty acid primary amide biosynthetic process; peptide amidation; and response to zinc ion. Predicted to be located in several cellular components, including perikaryon; secretory granule membrane; and trans-Golgi network. Predicted to be active in extracellular region. Is expressed in several structures, including alimentary system; central nervous system; forelimb bud; limb interdigital region; and sensory organ. Orthologous to human PAM (peptidylglycine alpha-amidating monooxygenase). [provided by Alliance of Genome Resources, Feb 2025]
Expression: Broad expression in heart adult (RPKM 108.5), adrenal adult (RPKM 50.3) and 22 other tissues See more
Orthologs: human all
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Genomic context

Location:: 1 D; 1 47.76 cM

Exon count:: 31

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	1	NC_000067.7 (97748816..98023578, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	1	NC_000067.6 (97821091..98095853, complement)

Chromosome 1 - NC_000067.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cell-type specific knockout of peptidylglycine alpha-amidating monooxygenase reveals specific behavioral roles in excitatory forebrain neurons and cardiomyocytes.
Title: Cell-type specific knockout of peptidylglycine α-amidating monooxygenase reveals specific behavioral roles in excitatory forebrain neurons and cardiomyocytes.
Peptidylglycine alpha-amidating mono-oxygenase serves as a luminal pH-sensor, regulating V-ATPase action by altering its assembly status in peptidergic cells.
Title: A pH-sensitive luminal His-cluster promotes interaction of PAM with V-ATPase along the secretory and endocytic pathways of peptidergic cells.
Results find that PAM colocalizes with actin but not microvilli in polarized multi-ciliated tracheal epithelial cells.
Title: Microvillar and ciliary defects in zebrafish lacking an actin-binding bioactive peptide amidating enzyme.
Oxygen Sensitivity of the Peptidylglycine alpha-Amidating Monooxygenase (PAM) in Neuroendocrine Cells
Title: Striking Oxygen Sensitivity of the Peptidylglycine α-Amidating Monooxygenase (PAM) in Neuroendocrine Cells.
Disruption of AP-1-dependent late endosomal trafficking diminishes the ability of PAM to retain copper and produce amidated peptides.
Title: Adaptor Protein-1 Complex Affects the Endocytic Trafficking and Function of Peptidylglycine α-Amidating Monooxygenase, a Luminal Cuproenzyme.
deficits in PAM reversibly affect copper homeostasis, with behavioral and physiological consequences
Title: Pam heterozygous mice reveal essential role for Cu in amygdalar behavioral and synaptic function.
Reduced amygdalar expression of Atox-1 and Atp7a in PAM heterozygous mice may lead to reduced synaptic Cu levels, contributing to the behavioral and neurochemical alterations seen in these mice.
Title: Peptidylglycine α-amidating monooxygenase heterozygosity alters brain copper handling with region specificity.
While glycine-extended reaction intermediates accumulated in the PAM(+/-) mice and reflected dietary copper availability, amidated products were far more prevalent under the conditions examined.
Title: Probing the production of amidated peptides following genetic and dietary copper manipulations.
Although the copper-dependent mechanisms through which the endocytic trafficking of PAM alters gene expression have not been elucidated in this review, the cytosolic fragment of PAM identified in pituitary and atrial nuclei is likely to play a key role.
Title: Peptidylgycine α-amidating monooxygenase and copper: a gene-nutrient interaction critical to nervous system function.
Cleavage of PAM releases a soluble CD fragment that localizes to the nucleus. Localization of PAM-CD to the nucleus was decreased when PAM-CD with phosphomimetic mutations was examined and when active Uhmk1 was simultaneously overexpressed.
Title: Signaling from the secretory granule to the nucleus: Uhmk1 and PAM.

Submit: New GeneRIF Correction See all GeneRIFs (13)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

U79523 (e-PCR)
- UniSTS:178444

Pam (e-PCR), detects polymorphism
- UniSTS:546918

BB187771 (e-PCR)
- UniSTS:185448

NoName (e-PCR)
- UniSTS:234182

NoName (e-PCR)
- UniSTS:225022

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables L-ascorbic acid binding	IEA Inferred from Electronic Annotation more info
enables calcium ion binding	ISO Inferred from Sequence Orthology more info
enables calcium ion binding	ISS Inferred from Sequence or Structural Similarity more info
enables copper ion binding	ISO Inferred from Sequence Orthology more info
enables copper ion binding	ISS Inferred from Sequence or Structural Similarity more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables peptidylamidoglycolate lyase activity	ISO Inferred from Sequence Orthology more info
enables peptidylamidoglycolate lyase activity	ISS Inferred from Sequence or Structural Similarity more info
enables peptidylglycine monooxygenase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidylglycine monooxygenase activity	ISO Inferred from Sequence Orthology more info
enables peptidylglycine monooxygenase activity	ISS Inferred from Sequence or Structural Similarity more info
enables peptidylglycine monooxygenase activity	TAS Traceable Author Statement more info	PubMed
enables protein kinase binding	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in fatty acid primary amide biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in fatty acid primary amide biosynthetic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in long-chain fatty acid metabolic process	ISO Inferred from Sequence Orthology more info
involved_in peptide amidation	ISO Inferred from Sequence Orthology more info
involved_in peptide amidation	ISS Inferred from Sequence or Structural Similarity more info
involved_in peptide metabolic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within peptide metabolic process	TAS Traceable Author Statement more info	PubMed
involved_in regulation of actin cytoskeleton organization	ISO Inferred from Sequence Orthology more info
involved_in regulation of transcription by RNA polymerase II	ISO Inferred from Sequence Orthology more info
involved_in response to pH	ISO Inferred from Sequence Orthology more info
involved_in response to xenobiotic stimulus	ISO Inferred from Sequence Orthology more info
involved_in response to zinc ion	IEA Inferred from Electronic Annotation more info
involved_in response to zinc ion	ISO Inferred from Sequence Orthology more info
involved_in toxin metabolic process	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in cytosol	TAS Traceable Author Statement more info	PubMed
is_active_in extracellular region	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in neuronal cell body	ISO Inferred from Sequence Orthology more info
located_in perikaryon	ISO Inferred from Sequence Orthology more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	TAS Traceable Author Statement more info	PubMed
located_in secretory granule	ISO Inferred from Sequence Orthology more info
located_in secretory granule membrane	ISS Inferred from Sequence or Structural Similarity more info
located_in trans-Golgi network	ISO Inferred from Sequence Orthology more info
located_in transport vesicle membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: peptidyl-glycine alpha-amidating monooxygenase

Names: PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE PRECURSOR (PAM)

NP_001344056.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407914.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407915.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407916.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407917.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407918.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407919.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407920.1

EC 1.14.17.3

EC 4.3.2.5

NP_001407921.1

EC 1.14.17.3

EC 4.3.2.5

NP_038654.2

EC 1.14.17.3

EC 4.3.2.5

XP_006529306.1

EC 1.14.17.3

EC 4.3.2.5

XP_011246239.1

EC 1.14.17.3

EC 4.3.2.5

XP_011246240.1

EC 1.14.17.3

EC 4.3.2.5

XP_011246241.1

EC 1.14.17.3

EC 4.3.2.5

XP_017174771.1

EC 1.14.17.3

EC 4.3.2.5

XP_017174773.1

EC 1.14.17.3

EC 4.3.2.5

XP_017174775.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108022.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108025.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108027.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108037.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108045.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108046.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108047.1

EC 1.14.17.3

EC 4.3.2.5

XP_030108050.1

EC 1.14.17.3

EC 4.3.2.5

XP_036018665.1

EC 1.14.17.3

EC 4.3.2.5

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001357127.2 → NP_001344056.1 peptidyl-glycine alpha-amidating monooxygenase isoform 2 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923

Consensus CDS

CCDS87863.1

UniProtKB/Swiss-Prot

E9QL07, P97467

Related

ENSMUSP00000057112.9, ENSMUST00000058762.15

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
NM_001420985.1 → NP_001407914.1 peptidyl-glycine alpha-amidating monooxygenase isoform 3 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923
NM_001420986.1 → NP_001407915.1 peptidyl-glycine alpha-amidating monooxygenase isoform 4 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923

UniProtKB/TrEMBL

E9Q704

Related

ENSMUSP00000125418.2, ENSMUST00000161567.8
NM_001420987.1 → NP_001407916.1 peptidyl-glycine alpha-amidating monooxygenase isoform 5 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923
NM_001420988.1 → NP_001407917.1 peptidyl-glycine alpha-amidating monooxygenase isoform 6 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923
NM_001420989.1 → NP_001407918.1 peptidyl-glycine alpha-amidating monooxygenase isoform 7 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923
NM_001420990.1 → NP_001407919.1 peptidyl-glycine alpha-amidating monooxygenase isoform 8 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923
NM_001420991.1 → NP_001407920.1 peptidyl-glycine alpha-amidating monooxygenase isoform 9 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923
NM_001420992.1 → NP_001407921.1 peptidyl-glycine alpha-amidating monooxygenase isoform 10 precursor

Status: VALIDATED

Source sequence(s)

AC102191, AC157923

UniProtKB/TrEMBL

F8VQA4
NM_013626.4 → NP_038654.2 peptidyl-glycine alpha-amidating monooxygenase isoform 1 precursor

See identical proteins and their annotated locations for NP_038654.2

Status: VALIDATED

Source sequence(s)

AC102191, AC157923

Consensus CDS

CCDS48331.1

UniProtKB/TrEMBL

F8VQA4

Related

ENSMUSP00000095228.4, ENSMUST00000097625.10

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:62 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000067.7 Reference GRCm39 C57BL/6J

Range

97748816..98023578 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_030252190.1 → XP_030108050.1 peptidyl-glycine alpha-amidating monooxygenase isoform X13

Conserved Domains (3) summary

cd14958
Location:397 → 704

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_030252187.1 → XP_030108047.1 peptidyl-glycine alpha-amidating monooxygenase isoform X12

Conserved Domains (3) summary

cd14958
Location:397 → 704

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_030252186.1 → XP_030108046.1 peptidyl-glycine alpha-amidating monooxygenase isoform X11

Conserved Domains (3) summary

cd14958
Location:397 → 704

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_030252185.1 → XP_030108045.1 peptidyl-glycine alpha-amidating monooxygenase isoform X10

Conserved Domains (3) summary

cd14958
Location:397 → 704

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_006529243.4 → XP_006529306.1 peptidyl-glycine alpha-amidating monooxygenase isoform X1

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_036162772.1 → XP_036018665.1 peptidyl-glycine alpha-amidating monooxygenase isoform X1

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_030252162.2 → XP_030108022.1 peptidyl-glycine alpha-amidating monooxygenase isoform X1

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_030252165.2 → XP_030108025.1 peptidyl-glycine alpha-amidating monooxygenase isoform X1

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_011247939.4 → XP_011246241.1 peptidyl-glycine alpha-amidating monooxygenase isoform X7

Conserved Domains (3) summary

cd14958
Location:397 → 704

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_017319286.3 → XP_017174775.1 peptidyl-glycine alpha-amidating monooxygenase isoform X5

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_011247938.4 → XP_011246240.1 peptidyl-glycine alpha-amidating monooxygenase isoform X4

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_011247937.4 → XP_011246239.1 peptidyl-glycine alpha-amidating monooxygenase isoform X2

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_017319284.3 → XP_017174773.1 peptidyl-glycine alpha-amidating monooxygenase isoform X3

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_030252167.1 → XP_030108027.1 peptidyl-glycine alpha-amidating monooxygenase isoform X1

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_030252177.1 → XP_030108037.1 peptidyl-glycine alpha-amidating monooxygenase isoform X7

Conserved Domains (3) summary

cd14958
Location:397 → 704

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain
XM_017319282.2 → XP_017174771.1 peptidyl-glycine alpha-amidating monooxygenase isoform X1

Conserved Domains (3) summary

cd14958
Location:503 → 810

NHL_PAL_like; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5)

pfam01082
Location:63 → 172

Cu2_monooxygen; Copper type II ascorbate-dependent monooxygenase, N-terminal domain

pfam03712
Location:200 → 346

Cu2_monoox_C; Copper type II ascorbate-dependent monooxygenase, C-terminal domain