PAM

Functionⁱ

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.1 Publication

Catalytic activityⁱ

Peptidylglycine + ascorbate + O₂ = peptidyl(2-hydroxyglycine) + dehydroascorbate + H₂O.

Peptidylamidoglycolate = peptidyl amide + glyoxylate.

Cofactorⁱ

Protein has several cofactor binding sites:

Zn²⁺By similarityNote: Zn²⁺ is required for the lyase reaction.By similarity
Cu²⁺By similarityNote: Binds 2 copper ions per subunit for the monooxygenase reaction.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	102	Copper ABy similarity	1
Metal bindingⁱ	103	Copper ABy similarity	1
Metal bindingⁱ	167	Copper ABy similarity	1
Metal bindingⁱ	237	Copper BBy similarity	1
Metal bindingⁱ	239	Copper BBy similarity	1
Metal bindingⁱ	309	Copper BBy similarity	1

GO - Molecular functionⁱ

copper ion binding Source: InterPro
L-ascorbic acid binding Source: UniProtKB-KW
peptidylamidoglycolate lyase activity Source: UniProtKB-EC
peptidylglycine monooxygenase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

peptide metabolic process Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase, Monooxygenase, Multifunctional enzyme, Oxidoreductase
Ligand	Copper, Metal-binding, Vitamin C, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Peptidyl-glycine alpha-amidating monooxygenase Short name: PAM Including the following 2 domains: Peptidylglycine alpha-hydroxylating monooxygenase (EC:1.14.17.3) Short name: PHM Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC:4.3.2.5) Alternative name(s): Peptidylamidoglycolate lyase Short name: PAL
Gene namesⁱ	Name:PAM
Organismⁱ	Bos taurus (Bovine)
Taxonomic identifierⁱ	9913 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
Proteomesⁱ	UP000009136 Componentⁱ: Unplaced

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	31 – 873	IntragranularSequence analysisAdd BLAST	843
Transmembraneⁱ	874 – 897	HelicalSequence analysisAdd BLAST	24
Topological domainⁱ	898 – 972	CytoplasmicSequence analysisAdd BLAST	75

Keywords - Cellular componentⁱ

Cytoplasmic vesicle, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 20	Sequence analysisAdd BLAST	20
PropeptideⁱPRO_0000006359	21 – 30	Sequence analysis	10
ChainⁱPRO_0000006360	31 – 972	Peptidyl-glycine alpha-amidating monooxygenaseAdd BLAST	942

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	42 ↔ 181	By similarity
Disulfide bondⁱ	76 ↔ 121	By similarity
Disulfide bondⁱ	109 ↔ 126	By similarity
Disulfide bondⁱ	222 ↔ 329	By similarity
Disulfide bondⁱ	288 ↔ 310	By similarity
Disulfide bondⁱ	631 ↔ 652	By similarity
Disulfide bondⁱ	699 ↔ 710	By similarity
Glycosylationⁱ	762	N-linked (GlcNAc...) asparagineSequence analysis	1
Modified residueⁱ	929	PhosphoserineBy similarity	1
Modified residueⁱ	942	PhosphoserineBy similarity	1
Modified residueⁱ	943	PhosphothreonineBy similarity	1
Modified residueⁱ	946	Phosphoserine; by UHMK1By similarity	1
Modified residueⁱ	957	PhosphoserineBy similarity	1

Keywords - PTMⁱ

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbⁱ	P10731.
PRIDEⁱ	P10731.

Interactionⁱ

Subunit structureⁱ

Monomer. Interacts with RASSF9 (By similarity).By similarity

Protein-protein interaction databases

IntActⁱ	P10731. 1 interactor.
Molecular INTeraction database More...MINTⁱ	P10731.
STRINGⁱ	9913.ENSBTAP00000016466.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P10731.
SMRⁱ	P10731.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	498 – 541	NHL 1Add BLAST	44
Repeatⁱ	567 – 608	NHL 2Add BLAST	42
Repeatⁱ	617 – 662	NHL 3Add BLAST	46
Repeatⁱ	670 – 714	NHL 4Add BLAST	45
Repeatⁱ	766 – 809	NHL 5Add BLAST	44

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 494	Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd BLAST	494
Regionⁱ	495 – 817	Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd BLAST	323
Regionⁱ	925 – 942	Interaction with RASSF9By similarityAdd BLAST	18

Sequence similaritiesⁱ

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.Curated

In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.Curated

Keywords - Domainⁱ

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3567. Eukaryota. ENOG410XS0X. LUCA.
HOGENOMⁱ	HOG000293368.
HOVERGENⁱ	HBG004218.
InParanoidⁱ	P10731.
KEGG Orthology (KO) More...KOⁱ	K00504. K18200.

Family and domain databases

Gene3Dⁱ	2.120.10.30. 1 hit. 2.60.120.230. 1 hit. 2.60.120.310. 1 hit.
InterProⁱ	View protein in InterPro IPR011042. 6-blade_b-propeller_TolB-like. IPR014784. Cu2_ascorb_mOase-like_C. IPR020611. Cu2_ascorb_mOase_CS-1. IPR014783. Cu2_ascorb_mOase_CS-2. IPR000323. Cu2_ascorb_mOase_N. IPR036939. Cu2_ascorb_mOase_N_sf. IPR024548. Cu2_monoox_C. IPR001258. NHL_repeat. IPR013017. NHL_repeat_subgr. IPR000720. PHM/PAL. IPR008977. PHM/PNGase_F_dom_sf.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03712. Cu2_monoox_C. 1 hit. PF01082. Cu2_monooxygen. 1 hit. PF01436. NHL. 3 hits.
PRINTSⁱ	PR00790. PAMONOXGNASE.
SUPFAMⁱ	SSF49742. SSF49742. 2 hits.
PROSITEⁱ	View protein in PROSITE PS00084. CU2_MONOOXYGENASE_1. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS51125. NHL. 5 hits.

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P10731-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAGFRSLLVL LLVFPSGCVG FRSPLSVFKR FKETTRSFSN ECLGTTRPVI 
        60         70         80         90        100
PIDSSDFALD IRMPGVTPKQ SDTYFCMSVR LPMDEEAFVI DFKPRASMDT 
       110        120        130        140        150
VHHMLLFGCN MPASTGNYWF CDEGTCTDKA NILYAWARNA PPTRLPKGVG 
       160        170        180        190        200
FRVGGETGSK YFVLQVHYGD ISAFRDNHKD CSGVSLHLTR LPQPLIAGMY 
       210        220        230        240        250
LMMSVDTVIP PGGKVVNSDI SCHYKKYPMH VFAYRVHTHH LGKVVSGYRV 
       260        270        280        290        300
RNGQWTLIGR QSPQLPQAFY PVEHPVDVSF GDILAARCVF TGEGRTEVTH 
       310        320        330        340        350
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDIFRT IPPEANIPIP 
       360        370        380        390        400
VKSDMVMMHG HHKETENKDK TSLLQQPKRE EEGVLEQGDF YSLLSKLLGE 
       410        420        430        440        450
REDVVHVHKY NPTEKAESES DLVAEIANVV QKKDLGRSDT RESAEQERGN 
       460        470        480        490        500
AILVRDRIHK FHRLVSTLRP AESRVLSLQQ PLPGEGTWEP EHTGDFHVEE 
       510        520        530        540        550
ALDWPGVYLL PGQVSGVALD PQNNLVIFHR GDHVWDGNSF DSKFVYQQRG 
       560        570        580        590        600
LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 
       610        620        630        640        650
QVFKLDPKSK EGPLLTLGRS MQPGSDQNHF CQPTDVAVDP DTGTIYVSDG 
       660        670        680        690        700
YCNSRLVQFS PSGKFITQWG EASLESSPKP GQFRVPHSLA LVPPLGQLCV 
       710        720        730        740        750
ADRENGRIQC FKTDTKEFVR EIKHPSFGRN VFAISYIPGL LFAVNGKPYF 
       760        770        780        790        800
EDQEPVQGFV MNFSSGEIID VFKPVRKHFD MPHDIAASED GTVYVGDAHT 
       810        820        830        840        850
NTVWKFTSTE KMEHRSVKKA GIEVQEIKES EAVVETKMEN KPASSELQKI 
       860        870        880        890        900
QEKQKLVKEP GSGVPAVLIT TLLVIPVVVL LAIALFIRWK KSRAFGDSER 
       910        920        930        940        950
KLEASSGRVL GRLRGKGGGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK 
       960        970 
DEDASESEEE YSAPPPAPAP SS

Length:972

Mass (Da):108,177

Last modified:April 1, 1993 - v2

Checksum:ⁱEBD41F83E341BAF1

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M18683 mRNA. Translation: AAA30683.1.
PIRⁱ	A40063. URBOAP.
NCBI Reference Sequences More...RefSeqⁱ	NP_776373.1. NM_173948.2.
UniGeneⁱ	Bt.12303.

Genome annotation databases

GeneIDⁱ	280890.
KEGGⁱ	bta:280890.

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P10731	UPI000766F16D A0A1U7U0P3 K9J661 A0A1U7TR29 UPI000B52B6F5 A0A1U7TFR0 UPI000B53395F UPI0004BDEE18 UPI0004BDFF11 UPI0005BD591A +90	Myotis davidii (David's myotis) Tarsius syrichta (Philippine tarsier) Desmodus rotundus (Vampire bat) Equus przewalskii (Przewalski's horse) (Equus caballus przewalskii) Pteropus vampyrus (Large flying fox) Pteropus alecto (Black flying fox) Myotis lucifugus (Little brown bat) Mustela putorius furo (European domestic ferret) (Mustela furo) Enhydra lutris kenyoni Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) And more	972	UniRef90_P10731	Cluster: Peptidyl-glycine alpha-amidating monooxygenase	101

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P10731	P14925 UPI000A321B76 UPI000A327A68 UPI000A321C58 UPI000A306600 P97467 UPI0005ABA4E0 UPI000A314F3E A0A287CS82 F8VQA4 +584	Rattus norvegicus (Rat) Mesocricetus auratus (Golden hamster) Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari) Mus musculus (Mouse) Mus caroli (Ryukyu mouse) (Ricefield mouse) Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus tridecemlineatus) Peromyscus maniculatus bairdii (Prairie deer mouse) Pteropus alecto (Black flying fox) Pteropus vampyrus (Large flying fox) Microtus ochrogaster (Prairie vole) And more	976	UniRef50_P14925	Cluster: Peptidyl-glycine alpha-amidating monooxygenase	595

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M18683 mRNA. Translation: AAA30683.1.
PIRⁱ	A40063. URBOAP.
NCBI Reference Sequences More...RefSeqⁱ	NP_776373.1. NM_173948.2.
UniGeneⁱ	Bt.12303.

3D structure databases

ProteinModelPortalⁱ	P10731.
SMRⁱ	P10731.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P10731. 1 interactor.
Molecular INTeraction database More...MINTⁱ	P10731.
STRINGⁱ	9913.ENSBTAP00000016466.

Proteomic databases

PaxDbⁱ	P10731.
PRIDEⁱ	P10731.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	280890.
KEGGⁱ	bta:280890.

Organism-specific databases

CTDⁱ	5066.

CTDⁱ

5066.

Phylogenomic databases

eggNOGⁱ	KOG3567. Eukaryota. ENOG410XS0X. LUCA.
HOGENOMⁱ	HOG000293368.
HOVERGENⁱ	HBG004218.
InParanoidⁱ	P10731.
KEGG Orthology (KO) More...KOⁱ	K00504. K18200.

Family and domain databases

Gene3Dⁱ	2.120.10.30. 1 hit. 2.60.120.230. 1 hit. 2.60.120.310. 1 hit.
InterProⁱ	View protein in InterPro IPR011042. 6-blade_b-propeller_TolB-like. IPR014784. Cu2_ascorb_mOase-like_C. IPR020611. Cu2_ascorb_mOase_CS-1. IPR014783. Cu2_ascorb_mOase_CS-2. IPR000323. Cu2_ascorb_mOase_N. IPR036939. Cu2_ascorb_mOase_N_sf. IPR024548. Cu2_monoox_C. IPR001258. NHL_repeat. IPR013017. NHL_repeat_subgr. IPR000720. PHM/PAL. IPR008977. PHM/PNGase_F_dom_sf.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03712. Cu2_monoox_C. 1 hit. PF01082. Cu2_monooxygen. 1 hit. PF01436. NHL. 3 hits.
PRINTSⁱ	PR00790. PAMONOXGNASE.
SUPFAMⁱ	SSF49742. SSF49742. 2 hits.
PROSITEⁱ	View protein in PROSITE PS00084. CU2_MONOOXYGENASE_1. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS51125. NHL. 5 hits.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AMD_BOVIN
Accessionⁱ	P10731Primary (citable) accession number: P10731
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	April 1, 1993
	Last modified:	March 28, 2018
	This is version 151 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

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UniParc

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UniProtKB - P10731 (AMD_BOVIN)

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Peptidyl-glycine alpha-amidating monooxygenase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Other locations

Other locations

Topology

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ