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P12890 (AMDB_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:

  1. Peptidylglycine alpha-hydroxylating monooxygenase B
    Short name=PHM-B
    EC=1.14.17.3
  2. Peptidyl-alpha-hydroxyglycine alpha-amidating lyase B
    EC=4.3.2.5
    Alternative name(s):
    Peptidylamidoglycolate lyase-B
    Short name=PAL-B
Gene names
Name:pam-b
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length875 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

Peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O.

Peptidylamidoglycolate = peptidyl amide + glyoxylate.

Cofactor

Zinc; for the lyase reaction By similarity.

Binds 2 copper ions per subunit; For the monoxygenase reaction By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasmic vesicle › secretory vesicle membrane; Single-pass membrane protein By similarity. Note: Secretory granules.

Sequence similarities

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.

In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

Contains 4 NHL repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Chain40 – 875836Peptidyl-glycine alpha-amidating monooxygenase B
PRO_0000006368

Regions

Topological domain40 – 763724Intragranular Potential
Transmembrane764 – 78724Helical; Potential
Topological domain788 – 87588Cytoplasmic Potential
Repeat467 – 50842NHL 1
Repeat516 – 56146NHL 2
Repeat569 – 61345NHL 3
Repeat666 – 70944NHL 4
Region3 – 394392Peptidylglycine alpha-hydroxylating monooxygenase By similarity
Region395 – 716322Peptidyl-alpha-hydroxyglycine alpha-amidating lyase By similarity

Sites

Metal binding1051Copper A By similarity
Metal binding1061Copper A By similarity
Metal binding1701Copper A By similarity
Metal binding2401Copper B By similarity
Metal binding2421Copper B By similarity
Metal binding3121Copper B By similarity

Amino acid modifications

Glycosylation4651N-linked (GlcNAc...) Potential
Glycosylation6621N-linked (GlcNAc...) Potential
Glycosylation7431N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 184 By similarity
Disulfide bond79 ↔ 124 By similarity
Disulfide bond112 ↔ 129 By similarity
Disulfide bond225 ↔ 332 By similarity
Disulfide bond291 ↔ 313 By similarity
Disulfide bond530 ↔ 551 By similarity
Disulfide bond598 ↔ 609 By similarity

Sequences

Sequence LengthMass (Da)Tools
P12890 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: C07373AF6BF13450

FASTA87597,085
        10         20         30         40         50         60 
MDMASLISSL LVLFLIFQNS CYCFRSPLSV FKRYEESTRS LSNDCLGTTR PVMSPGSSDY 

        70         80         90        100        110        120 
TLDIRMPGVT PTESDTYLCK SYRLPVDDEA YVVDYRPHAN MDTAHHMLLF GCNVPSSTDD 

       130        140        150        160        170        180 
YWDCSAGTCN DKSSIMYAWA KNAPPTKLPE GVGFQVGGKS GSRYFVLQVH YGDVKAFQDK 

       190        200        210        220        230        240 
HKDCTGVTVR ITPEKQPLIA GIYLSMSLNT VVPPGQEVVN SDIACLYNRP TIHPFAYRVH 

       250        260        270        280        290        300 
THQLGQVVSG FRVRHGKWTL IGRQSPQLPQ AFYPVEHPLE ISPGDIIATR CLFTGKGRMS 

       310        320        330        340        350        360 
ATYIGGTAKD EMCNLYIMYY MDAAHATSYM TCVQTGNPKL FENIPEIANV PIPVSPDMMM 

       370        380        390        400        410        420 
MMMMGHGHHH TEAEAETNTA LQQPKREEEE VLNQDVHLEE DTDWPGVNLK VGQVSGLALD 

       430        440        450        460        470        480 
PKNNLVIFHR GDHVWDENSF DRNFVYQQRG IGPIQESTIL VVDPNTSKVL KSTGQNLFFL 

       490        500        510        520        530        540 
PHGLTIDRDG NYWVTDVALH QVFKVGAEKE TPLLVLGRAF QPGSDRKHFC QPTDVAVDPI 

       550        560        570        580        590        600 
TGNFFVADGY CNSRIMQFSP NGMFIMQWGE ETSSNLPRPG QFRIPHSLTM ISDQGQLCVA 

       610        620        630        640        650        660 
DRENGRIQCF HAKTGEFVKQ IKHQEFGREV FAVSYAPGGV LYAVNGKPYY GDSTPVQGFM 

       670        680        690        700        710        720 
LNFSNGDILD TFIPARKNFE MPHDIAAGDD GTVYVGDAHA NAVWKFSPSK AEHRSVKKAG 

       730        740        750        760        770        780 
IEVEEITETE IFETHMRSRP KTNESVGQQT QEKPSVVQES SAGVSFVLII TLLIIPVVVL 

       790        800        810        820        830        840 
IAIAIFIRWR KVRMYGGDIG HKSESSSGGI LGKLRGKGSG GLNLGTFFAT HKGYSRKGFD 

       850        860        870 
RLSTEGSDQE KDDDDDGSDS EEEYSAPPIP PVSSS

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References

[1]"Cloning of cDNA encoding a new peptide C-terminal alpha-amidating enzyme having a putative membrane-spanning domain from Xenopus laevis skin."
Ohsuye K., Kitano K., Wada Y., Fuchimura K., Tanaka S., Mizuno K., Matsuo H.
Biochem. Biophys. Res. Commun. 150:1275-1281(1988) [PubMed: 2829895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M19032 mRNA. Translation: AAA49667.1.
PIRURXLA2. A27715.
RefSeqNP_001081254.1. NM_001087785.1.
UniGeneXl.536.

3D structure databases

ProteinModelPortalP12890.
SMRP12890. Positions 43-354.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397736.
KEGGxla:397736.

Organism-specific databases

CTD397736.
XenbaseXB-GENE-6252615. pam.

Phylogenomic databases

HOVERGENHBG004218.

Family and domain databases

InterProIPR011042. 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.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000720. Pep_amidat_mOase.
IPR008977. PHM/PNGase_F_dom.
[Graphical view]
Gene3DG3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
G3DSA:2.60.120.230. Cu2_ascorb_mOase_core. 1 hit.
G3DSA:2.60.120.310. Cu2_ascorb_mOase_core. 1 hit.
KOK00504.
PfamPF01082. Cu2_monooxygen. 1 hit.
PF01436. NHL. 4 hits.
[Graphical view]
PRINTSPR00790. PAMONOXGNASE.
SUPFAMSSF49742. PHM_PNGase_F. 2 hits.
PROSITEPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS51125. NHL. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMDB_XENLA
AccessionPrimary (citable) accession number: P12890
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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