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Protein

Peptidyl-glycine alpha-amidating monooxygenase

Gene

PAM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 monoxygenase reaction.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021Copper ABy similarity
Metal bindingi103 – 1031Copper ABy similarity
Metal bindingi167 – 1671Copper ABy similarity
Metal bindingi237 – 2371Copper BBy similarity
Metal bindingi239 – 2391Copper BBy similarity
Metal bindingi309 – 3091Copper BBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Ligandi

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 873843IntragranularSequence analysisAdd
BLAST
Transmembranei874 – 89724HelicalSequence analysisAdd
BLAST
Topological domaini898 – 97275CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 3010Sequence analysisPRO_0000006359
Chaini31 – 972942Peptidyl-glycine alpha-amidating monooxygenasePRO_0000006360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 181By similarity
Disulfide bondi76 ↔ 121By similarity
Disulfide bondi109 ↔ 126By similarity
Disulfide bondi222 ↔ 329By similarity
Disulfide bondi288 ↔ 310By similarity
Disulfide bondi631 ↔ 652By similarity
Disulfide bondi699 ↔ 710By similarity
Glycosylationi762 – 7621N-linked (GlcNAc...)Sequence analysis
Modified residuei929 – 9291PhosphoserineBy similarity
Modified residuei942 – 9421PhosphoserineBy similarity
Modified residuei943 – 9431PhosphothreonineBy similarity
Modified residuei946 – 9461Phosphoserine; by UHMK1By similarity
Modified residuei957 – 9571PhosphoserineBy similarity
Modified residuei961 – 9611SulfotyrosineBy similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP10731.
PRIDEiP10731.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

MINTiMINT-1365422.
STRINGi9913.ENSBTAP00000016466.

Structurei

3D structure databases

ProteinModelPortaliP10731.
SMRiP10731. Positions 40-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati498 – 54144NHL 1Add
BLAST
Repeati567 – 60842NHL 2Add
BLAST
Repeati617 – 66246NHL 3Add
BLAST
Repeati670 – 71445NHL 4Add
BLAST
Repeati766 – 80944NHL 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 494494Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd
BLAST
Regioni495 – 817323Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd
BLAST
Regioni925 – 94218Interaction with RASSF9By similarityAdd
BLAST

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
Contains 5 NHL repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3567. Eukaryota.
ENOG410XS0X. LUCA.
HOGENOMiHOG000293368.
HOVERGENiHBG004218.
InParanoidiP10731.
KOiK00504.
K18200.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR011042. 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.
IPR024548. Cu2_monoox_C.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000720. PHM/PAL.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 3 hits.
[Graphical view]
PRINTSiPR00790. PAMONOXGNASE.
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10731-1 [UniParc]FASTAAdd 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.
PIRiA40063. URBOAP.
RefSeqiNP_776373.1. NM_173948.2.
UniGeneiBt.12303.

Genome annotation databases

GeneIDi280890.
KEGGibta:280890.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18683 mRNA. Translation: AAA30683.1.
PIRiA40063. URBOAP.
RefSeqiNP_776373.1. NM_173948.2.
UniGeneiBt.12303.

3D structure databases

ProteinModelPortaliP10731.
SMRiP10731. Positions 40-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1365422.
STRINGi9913.ENSBTAP00000016466.

Proteomic databases

PaxDbiP10731.
PRIDEiP10731.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280890.
KEGGibta:280890.

Organism-specific databases

CTDi5066.

Phylogenomic databases

eggNOGiKOG3567. Eukaryota.
ENOG410XS0X. LUCA.
HOGENOMiHOG000293368.
HOVERGENiHBG004218.
InParanoidiP10731.
KOiK00504.
K18200.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR011042. 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.
IPR024548. Cu2_monoox_C.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000720. PHM/PAL.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 3 hits.
[Graphical view]
PRINTSiPR00790. PAMONOXGNASE.
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMD_BOVIN
AccessioniPrimary (citable) accession number: P10731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1993
Last modified: June 8, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.