Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-glycine alpha-amidating monooxygenase A

Gene

pam-a

Organism
Xenopus laevis (African clawed frog)
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 monooxygenase reaction.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi103Copper ABy similarity1
Metal bindingi104Copper ABy similarity1
Metal bindingi168Copper ABy similarity1
Metal bindingi238Copper BBy similarity1
Metal bindingi240Copper BBy similarity1
Metal bindingi310Copper BBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-glycine alpha-amidating monooxygenase A
Short 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:
Peptidylglycine alpha-hydroxylating monooxygenase A (EC:1.14.17.3)
Short name:
PHM-A
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase A (EC:4.3.2.5)
Alternative name(s):
Peptidylamidoglycolate lyase-A
Short name:
PAL-A
Gene namesi
Name:pam-a
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-950939. pam.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini37 – 825IntragranularSequence analysisAdd BLAST789
Transmembranei826 – 846HelicalSequence analysisAdd BLAST21
Topological domaini847 – 935CytoplasmicSequence analysisAdd BLAST89

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000000636737 – 935Peptidyl-glycine alpha-amidating monooxygenase AAdd BLAST899

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi43 ↔ 182By similarity
Disulfide bondi77 ↔ 122By similarity
Disulfide bondi110 ↔ 127By similarity
Disulfide bondi223 ↔ 330By similarity
Disulfide bondi289 ↔ 311By similarity
Disulfide bondi526 ↔ 547By similarity
Disulfide bondi594 ↔ 605By similarity
Glycosylationi658N-linked (GlcNAc...)Sequence analysis1
Glycosylationi739N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP08478.

Interactioni

Subunit structurei

Monomer.By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati463 – 504NHL 1Add BLAST42
Repeati512 – 557NHL 2Add BLAST46
Repeati565 – 609NHL 3Add BLAST45
Repeati662 – 705NHL 4Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 390Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd BLAST390
Regioni391 – 712Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd BLAST322

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 4 NHL repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG004218.
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. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08478-1) [UniParc]FASTAAdd to basket
Also known as: AE-III

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Length:935
Mass (Da):103,389
Last modified:March 23, 2010 - v3
Checksum:iE9C2BF75733AB83C
GO
Isoform 2 (identifier: P08478-2) [UniParc]FASTAAdd to basket
Also known as: AE-I

The sequence of this isoform differs from the canonical sequence as follows:
     391-400: DVHLEEDTDW → GLITLGDSAV
     401-935: Missing.

Show »
Length:400
Mass (Da):44,457
Checksum:iFE4E8FA261D1EA33
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti792P → S in CAA44615 (PubMed:1935950).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_020312391 – 400DVHLEEDTDW → GLITLGDSAV in isoform 2. 2 Publications10
Alternative sequenceiVSP_020313401 – 935Missing in isoform 2. 2 PublicationsAdd BLAST535

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.
PIRiA29726. URXLA1.
S17855.
RefSeqiNP_001079520.2. NM_001086051.2.
UniGeneiXl.417.

Genome annotation databases

GeneIDi379207.
KEGGixla:379207.

Keywords - Coding sequence diversityi

Alternative splicing

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.
PIRiA29726. URXLA1.
S17855.
RefSeqiNP_001079520.2. NM_001086051.2.
UniGeneiXl.417.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP08478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi379207.
KEGGixla:379207.

Organism-specific databases

CTDi379207.
XenbaseiXB-GENE-950939. pam.

Phylogenomic databases

HOVERGENiHBG004218.
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. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMDA_XENLA
AccessioniPrimary (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: November 30, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Multifunctional enzyme

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.