Reviewed, UniProtKB/Swiss-Prot P12890 (AMD2_XENLA)

Names and origin

Protein names

Recommended name:
    Peptidyl-glycine alpha-amidating monooxygenase B
      Short name=PAM-B
Alternative name(s):
    Peptidyl-glycine alpha-amidating monooxygenase II
    Peptide C-terminal alpha-amidating enzyme II
      Short name=AE-II
Including the following 2 domains:
    1- Recommended name:
            Peptidylglycine alpha-hydroxylating monooxygenase B
                Short name=PHM-B
              EC=1.14.17.3
    2- Recommended name:
            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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	875 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes 2 sequencial 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 + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. 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 proteinBy 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.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane
Domain	Repeat Signal Transmembrane
Ligand	Copper Metal-binding Zinc
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro peptidylamidoglycolate lyase activity Inferred from electronic annotation. Source: EC peptidylglycine monooxygenase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 39	39	Potential
	Chain	40 – 875	836	Peptidyl-glycine alpha-amidating monooxygenase B		PRO_0000006368
Regions
	Topological domain	40 – 763	724	Intragranular Potential
	Transmembrane	764 – 787	24	Potential
	Topological domain	788 – 875	88	Cytoplasmic Potential
	Repeat	467 – 508	42	NHL 1
	Repeat	516 – 561	46	NHL 2
	Repeat	569 – 613	45	NHL 3
	Repeat	666 – 709	44	NHL 4
	Region	3 – 394	392	Peptidylglycine alpha-hydroxylating monooxygenase By similarity
	Region	395 – 716	322	Peptidyl-alpha-hydroxyglycine alpha-amidating lyase By similarity
Sites
	Metal binding	105	1	Copper A By similarity
	Metal binding	106	1	Copper A By similarity
	Metal binding	170	1	Copper A By similarity
	Metal binding	240	1	Copper B By similarity
	Metal binding	242	1	Copper B By similarity
	Metal binding	312	1	Copper B By similarity
Amino acid modifications
	Glycosylation	465	1	N-linked (GlcNAc...) Potential
	Glycosylation	662	1	N-linked (GlcNAc...) Potential
	Glycosylation	743	1	N-linked (GlcNAc...) Potential
	Disulfide bond	45 ↔ 184		By similarity
	Disulfide bond	79 ↔ 124		By similarity
	Disulfide bond	112 ↔ 129		By similarity
	Disulfide bond	225 ↔ 332		By similarity
	Disulfide bond	291 ↔ 313		By similarity
	Disulfide bond	530 ↔ 551		By similarity
	Disulfide bond	598 ↔ 609		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12890-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: C07373AF6BF13450	FASTA	875	97,085
	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M19032 mRNA. Translation: AAA49667.1.
PIR	URXLA2. A27715.
RefSeq	NP_001081254.1.
UniGene	Xl.536
3D structure databases
HSSP	HSSP built from PDB template 1PHM based on UniProtKB P14925.
ModBase	Search...
Genome annotation databases
GeneID	397736.
KEGG	xla:397736.
Phylogenomic databases
HOVERGEN	P12890.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR014783. Cu2_ascorb_mOase_C. IPR014784. Cu2_ascorb_mOase_like_C. IPR000323. Cu2_ascorb_mOase_N. IPR001258. NHL_repeat. IPR013017. NHL_repeat_subgr. IPR000720. Pep_amidat_mOase. [Graphical view]
Gene3D	G3DSA: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.
Pfam	PF03712. Cu2_monoox_C. 1 hit. PF01082. Cu2_monooxygen. 1 hit. PF01436. NHL. 4 hits. [Graphical view]
PRINTS	PR00790. PAMONOXGNASE.
PROSITE	PS00084. CU2_MONOOXYGENASE_1. 1 hit. PS00085. CU2_MONOOXYGENASE_2. 1 hit. PS51125. NHL. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMD2_XENLA

Accession

Primary (citable) accession number: P12890

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project