UniProtKB - P10731 (AMD_BOVIN)
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Protein
Peptidyl-glycine alpha-amidating monooxygenase
Gene
PAM
Organism
Bos taurus (Bovine)
Status
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 | Graphical view | 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
GO - Biological processi
- peptide metabolic process Source: InterPro
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 monooxygenaseShort name: PAM Including the following 2 domains: |
Gene namesi | Name:PAM |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | 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, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | 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 | Graphical view | 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, PhosphoproteinProteomic databases
PaxDbi | P10731. |
PRIDEi | P10731. |
Interactioni
Subunit structurei
Monomer. Interacts with RASSF9 (By similarity).By similarity
Protein-protein interaction databases
IntActi | P10731. 1 interactor. |
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 | Graphical view | 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 | Graphical view | 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 helixPhylogenomic databases
eggNOGi | KOG3567. Eukaryota. ENOG410XS0X. LUCA. |
HOGENOMi | HOG000293368. |
HOVERGENi | HBG004218. |
InParanoidi | P10731. |
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. |
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. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P10731-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18683 mRNA. Translation: AAA30683.1. |
PIRi | A40063. URBOAP. |
RefSeqi | NP_776373.1. NM_173948.2. |
UniGenei | Bt.12303. |
Genome annotation databases
GeneIDi | 280890. |
KEGGi | bta:280890. |
Similar proteinsi
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 |