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Entry version 125 (02 Jun 2021)
Sequence version 1 (01 Oct 1989)
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Protein

Peptidyl-glycine alpha-amidating monooxygenase B

Gene

pam-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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 (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi105Copper ABy similarity1
Metal bindingi106Copper ABy similarity1
Metal bindingi170Copper ABy similarity1
Metal bindingi240Copper BBy similarity1
Metal bindingi242Copper BBy similarity1
Metal bindingi312Copper BBy similarity1

<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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase, Monooxygenase, Multifunctional enzyme, Oxidoreductase
LigandCopper, Metal-binding, Zinc

<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 subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Peptidyl-glycine alpha-amidating monooxygenase B
Short name:
PAM-B
Alternative name(s):
Peptide C-terminal alpha-amidating enzyme II
Short name:
AE-II
Peptidyl-glycine alpha-amidating monooxygenase II
Including the following 2 domains:
Peptidylglycine alpha-hydroxylating monooxygenase B (EC:1.14.17.3)
Short name:
PHM-B
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase B (EC:4.3.2.5)
Alternative name(s):
Peptidylamidoglycolate lyase-B
Short name:
PAL-B
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:pam-b
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-6252615, pam.S

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini40 – 763IntragranularSequence analysisAdd BLAST724
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei764 – 787HelicalSequence analysisAdd BLAST24
Topological domaini788 – 875CytoplasmicSequence analysisAdd BLAST88

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 39Sequence analysisAdd BLAST39
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000636840 – 875Peptidyl-glycine alpha-amidating monooxygenase BAdd BLAST836

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi45 ↔ 184By similarity
Disulfide bondi79 ↔ 124By similarity
Disulfide bondi112 ↔ 129By similarity
Disulfide bondi225 ↔ 332By similarity
Disulfide bondi291 ↔ 313By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi465N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi530 ↔ 551By similarity
Disulfide bondi598 ↔ 609By similarity
Glycosylationi662N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi743N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

By similarity

<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

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P12890

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati467 – 508NHL 1Add BLAST42
Repeati516 – 561NHL 2Add BLAST46
Repeati569 – 613NHL 3Add BLAST45
Repeati666 – 709NHL 4Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni3 – 394Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd BLAST392
Regioni395 – 716Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd BLAST322
Regioni735 – 755DisorderedSequence analysisAdd BLAST21
Regioni837 – 875DisorderedSequence analysisAdd BLAST39

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi741 – 755Polar residuesSequence analysisAdd BLAST15

<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

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

Database of Orthologous Groups

More...
OrthoDBi
476471at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.120.10.30, 1 hit
2.60.120.230, 1 hit
2.60.120.310, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00790, PAMONOXGNASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49742, SSF49742, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00084, CU2_MONOOXYGENASE_1, 1 hit
PS00085, CU2_MONOOXYGENASE_2, 1 hit
PS51125, NHL, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P12890-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDMASLISSL LVLFLIFQNS CYCFRSPLSV FKRYEESTRS LSNDCLGTTR
60 70 80 90 100
PVMSPGSSDY TLDIRMPGVT PTESDTYLCK SYRLPVDDEA YVVDYRPHAN
110 120 130 140 150
MDTAHHMLLF GCNVPSSTDD YWDCSAGTCN DKSSIMYAWA KNAPPTKLPE
160 170 180 190 200
GVGFQVGGKS GSRYFVLQVH YGDVKAFQDK HKDCTGVTVR ITPEKQPLIA
210 220 230 240 250
GIYLSMSLNT VVPPGQEVVN SDIACLYNRP TIHPFAYRVH THQLGQVVSG
260 270 280 290 300
FRVRHGKWTL IGRQSPQLPQ AFYPVEHPLE ISPGDIIATR CLFTGKGRMS
310 320 330 340 350
ATYIGGTAKD EMCNLYIMYY MDAAHATSYM TCVQTGNPKL FENIPEIANV
360 370 380 390 400
PIPVSPDMMM MMMMGHGHHH TEAEAETNTA LQQPKREEEE VLNQDVHLEE
410 420 430 440 450
DTDWPGVNLK VGQVSGLALD PKNNLVIFHR GDHVWDENSF DRNFVYQQRG
460 470 480 490 500
IGPIQESTIL VVDPNTSKVL KSTGQNLFFL PHGLTIDRDG NYWVTDVALH
510 520 530 540 550
QVFKVGAEKE TPLLVLGRAF QPGSDRKHFC QPTDVAVDPI TGNFFVADGY
560 570 580 590 600
CNSRIMQFSP NGMFIMQWGE ETSSNLPRPG QFRIPHSLTM ISDQGQLCVA
610 620 630 640 650
DRENGRIQCF HAKTGEFVKQ IKHQEFGREV FAVSYAPGGV LYAVNGKPYY
660 670 680 690 700
GDSTPVQGFM LNFSNGDILD TFIPARKNFE MPHDIAAGDD GTVYVGDAHA
710 720 730 740 750
NAVWKFSPSK AEHRSVKKAG IEVEEITETE IFETHMRSRP KTNESVGQQT
760 770 780 790 800
QEKPSVVQES SAGVSFVLII TLLIIPVVVL IAIAIFIRWR KVRMYGGDIG
810 820 830 840 850
HKSESSSGGI LGKLRGKGSG GLNLGTFFAT HKGYSRKGFD RLSTEGSDQE
860 870
KDDDDDGSDS EEEYSAPPIP PVSSS
Length:875
Mass (Da):97,085
Last modified:October 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC07373AF6BF13450
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M19032 mRNA Translation: AAA49667.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A27715, URXLA2

NCBI Reference Sequences

More...
RefSeqi
NP_001081254.1, NM_001087785.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
397736

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:397736

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19032 mRNA Translation: AAA49667.1
PIRiA27715, URXLA2
RefSeqiNP_001081254.1, NM_001087785.1

3D structure databases

SMRiP12890
ModBaseiSearch...

Genome annotation databases

GeneIDi397736
KEGGixla:397736

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
397736
XenbaseiXB-GENE-6252615, pam.S

Phylogenomic databases

OrthoDBi476471at2759

Family and domain databases

Gene3Di2.120.10.30, 1 hit
2.60.120.230, 1 hit
2.60.120.310, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF03712, Cu2_monoox_C, 1 hit
PF01082, Cu2_monooxygen, 1 hit
PF01436, NHL, 3 hits
PRINTSiPR00790, PAMONOXGNASE
SUPFAMiSSF49742, SSF49742, 2 hits
PROSITEiView protein in PROSITE
PS00084, CU2_MONOOXYGENASE_1, 1 hit
PS00085, CU2_MONOOXYGENASE_2, 1 hit
PS51125, NHL, 4 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMDB_XENLA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P12890
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 2, 2021
This is version 125 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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