UniProtKB - P08478 (AMDA_XENLA)
Peptidyl-glycine alpha-amidating monooxygenase A
pam-a
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 PublicationCatalytic activityi
- a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radicalEC:1.14.17.3
- EC:4.3.2.5
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 | 103 | Copper ABy similarity | 1 | |
Metal bindingi | 104 | Copper ABy similarity | 1 | |
Metal bindingi | 168 | Copper ABy similarity | 1 | |
Metal bindingi | 238 | Copper BBy similarity | 1 | |
Metal bindingi | 240 | Copper BBy similarity | 1 | |
Metal bindingi | 310 | Copper BBy similarity | 1 |
GO - Molecular functioni
- copper ion binding Source: InterPro
- 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, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: Peptidyl-glycine alpha-amidating monooxygenase AShort name: PAM-A Alternative name(s): Peptide C-terminal alpha-amidating enzyme I Short name: AE-I Peptidyl-glycine alpha-amidating monooxygenase I Including the following 2 domains: |
Gene namesi | Name:pam-a |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Proteomesi |
|
Organism-specific databases
Xenbasei | XB-GENE-950939, pam.L |
Subcellular locationi
Other locations
- secretory vesicle membrane By similarity; Single-pass membrane protein By similarity
Note: Secretory granules.
Other locations
- integral component of membrane Source: UniProtKB-KW
- transport vesicle membrane Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 37 – 825 | IntragranularSequence analysisAdd BLAST | 789 | |
Transmembranei | 826 – 846 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 847 – 935 | CytoplasmicSequence analysisAdd BLAST | 89 |
Keywords - Cellular componenti
Cytoplasmic vesicle, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 36 | Sequence analysisAdd BLAST | 36 | |
ChainiPRO_0000006367 | 37 – 935 | Peptidyl-glycine alpha-amidating monooxygenase AAdd BLAST | 899 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 43 ↔ 182 | By similarity | ||
Disulfide bondi | 77 ↔ 122 | By similarity | ||
Disulfide bondi | 110 ↔ 127 | By similarity | ||
Disulfide bondi | 223 ↔ 330 | By similarity | ||
Disulfide bondi | 289 ↔ 311 | By similarity | ||
Disulfide bondi | 526 ↔ 547 | By similarity | ||
Disulfide bondi | 594 ↔ 605 | By similarity | ||
Glycosylationi | 658 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 739 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PRIDEi | P08478 |
Interactioni
Subunit structurei
Monomer.
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 463 – 504 | NHL 1Add BLAST | 42 | |
Repeati | 512 – 557 | NHL 2Add BLAST | 46 | |
Repeati | 565 – 609 | NHL 3Add BLAST | 45 | |
Repeati | 662 – 705 | NHL 4Add BLAST | 44 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 390 | Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd BLAST | 390 | |
Regioni | 362 – 385 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 391 – 712 | Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd BLAST | 322 | |
Regioni | 728 – 764 | DisorderedSequence analysisAdd BLAST | 37 | |
Regioni | 778 – 812 | DisorderedSequence analysisAdd BLAST | 35 | |
Regioni | 896 – 935 | DisorderedSequence analysisAdd BLAST | 40 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 728 – 750 | Basic and acidic residuesSequence analysisAdd BLAST | 23 |
Sequence similaritiesi
Keywords - Domaini
Repeat, Signal, Transmembrane, Transmembrane helixFamily 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 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, 4 hits |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MASLSSSFLV LFLLFQNSCY CFRSPLSVFK RYEESTRSLS NDCLGTTRPV
60 70 80 90 100
MSPGSSDYTL DIRMPGVTPT ESDTYLCKSY RLPVDDEAYV VDFRPHANMD
110 120 130 140 150
TAHHMLLFGC NIPSSTDDYW DCSAGTCMDK SSIMYAWAKN APPTKLPEGV
160 170 180 190 200
GFRVGGKSGS RYFVLQVHYG NVKAFQDKHK DCTGVTVRVT PEKQPQIAGI
210 220 230 240 250
YLSMSVDTVI PPGEEAVNSD IACLYNRPTI HPFAYRVHTH QLGQVVSGFR
260 270 280 290 300
VRHGKWSLIG RQSPQLPQAF YPVEHPVEIS PGDIIATRCL FTGKGRTSAT
310 320 330 340 350
YIGGTSNDEM CNLYIMYYMD AAHATSYMTC VQTGEPKLFQ NIPEIANVPI
360 370 380 390 400
PVSPDMMMMM GHGHHHTEAE PEKNTGLQQP KREEEEVLDQ DVHLEEDTDW
410 420 430 440 450
PGVNLKVGQV SGLALDPKNN LAIFHRGDHV WDENSFDRNF VYQQRGIGPI
460 470 480 490 500
QESTILVVDP SSSKVLKSTG KNLFFLPHGL TIDRDGNYWV TDVALHQVFK
510 520 530 540 550
LGAGKETPLL VLGRAFQPGS DRKHFCQPTD VAVDPITGNF FVADGYCNSR
560 570 580 590 600
IMQFSPNGMF IMQWGEETSS NVPRPGQFRI PHSLTMVPDQ GQLCVADREN
610 620 630 640 650
GRIQCFHAET GNFVKQIKHQ EFGREVFAVS YAPGGVLYAV NGKPYYGYSA
660 670 680 690 700
PVQGFMLNFS NGDILDTFIP ARKNFDMPHD IAAADDGTVY VGDAHANAVW
710 720 730 740 750
KFSPSKAEHR SVKKAGIEVE EITETEIFET HIRSRPKTNE SVEKQTQEKQ
760 770 780 790 800
QKQKNSAGVS TQEKQNVVQE INAGVPTQEK QNVVQESSAG VPTQEKQSVV
810 820 830 840 850
QESSAGVSTQ EKQSVVQESS AGVSFVLIIT LLIIPIAVLI AIAIFIRWRK
860 870 880 890 900
VRMYGGDIDH KSESSSVGIL GKLRGKGSGG LNLGTFFATH KGYSRKGFDR
910 920 930
LSTEGSDQEK DDDDGSDSEE EYSAPPIPPA PVSSS
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 792 | P → S in CAA44615 (PubMed:1935950).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_020312 | 391 – 400 | DVHLEEDTDW → GLITLGDSAV in isoform 2. 2 Publications | 10 | |
Alternative sequenceiVSP_020313 | 401 – 935 | Missing in isoform 2. 2 PublicationsAdd BLAST | 535 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18134 mRNA Translation: AAA49640.1 X62771 mRNA Translation: CAA44615.1 BC043987 mRNA Translation: AAH43987.1 BC170012 mRNA Translation: AAI70012.1 BC170016 mRNA Translation: AAI70016.1 |
PIRi | A29726, URXLA1 S17855 |
RefSeqi | NP_001079520.2, NM_001086051.2 |
Genome annotation databases
GeneIDi | 379207 |
KEGGi | xla:379207 |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18134 mRNA Translation: AAA49640.1 X62771 mRNA Translation: CAA44615.1 BC043987 mRNA Translation: AAH43987.1 BC170012 mRNA Translation: AAI70012.1 BC170016 mRNA Translation: AAI70016.1 |
PIRi | A29726, URXLA1 S17855 |
RefSeqi | NP_001079520.2, NM_001086051.2 |
3D structure databases
AlphaFoldDBi | P08478 |
SMRi | P08478 |
ModBasei | Search... |
Proteomic databases
PRIDEi | P08478 |
Genome annotation databases
GeneIDi | 379207 |
KEGGi | xla:379207 |
Organism-specific databases
CTDi | 379207 |
Xenbasei | XB-GENE-950939, pam.L |
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 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, 4 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | AMDA_XENLA | |
Accessioni | P08478Primary (citable) accession number: P08478 Secondary accession number(s): B7ZR22, Q5D0B6, Q91697 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | March 23, 2010 | |
Last modified: | May 25, 2022 | |
This is version 129 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families