AMDB_XENLA
ID AMDB_XENLA Reviewed; 875 AA.
AC P12890;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Peptidyl-glycine alpha-amidating monooxygenase B;
DE Short=PAM-B;
DE AltName: Full=Peptide C-terminal alpha-amidating enzyme II;
DE Short=AE-II;
DE AltName: Full=Peptidyl-glycine alpha-amidating monooxygenase II;
DE Includes:
DE RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase B;
DE Short=PHM-B;
DE EC=1.14.17.3;
DE Includes:
DE RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase B;
DE EC=4.3.2.5;
DE AltName: Full=Peptidylamidoglycolate lyase-B;
DE Short=PAL-B;
DE Flags: Precursor;
GN Name=pam-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=2829895; DOI=10.1016/0006-291x(88)90767-x;
RA Ohsuye K., Kitano K., Wada Y., Fuchimura K., Tanaka S., Mizuno K.,
RA Matsuo H.;
RT "Cloning of cDNA encoding a new peptide C-terminal alpha-amidating enzyme
RT having a putative membrane-spanning domain from Xenopus laevis skin.";
RL Biochem. Biophys. Res. Commun. 150:1275-1281(1988).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in C-
CC terminal alpha-amidation of peptides. The monooxygenase part produces
CC an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated
CC to glyoxylate and the corresponding desglycine peptide amide by the
CC lyase part. C-terminal amidation of peptides such as neuropeptides is
CC essential for full biological activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a
CC [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-
CC ascorbate radical; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486,
CC Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:CHEBI:137000,
CC ChEBI:CHEBI:142768; EC=1.14.17.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-
CC terminal amide + glyoxylate; Xref=Rhea:RHEA:20924, Rhea:RHEA-
CC COMP:13485, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:137001, ChEBI:CHEBI:142768; EC=4.3.2.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Zn(2+) is required for the lyase reaction. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per subunit for the monooxygenase reaction.
CC {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Note=Secretory granules.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl-alpha-
CC hydroxyglycine alpha-amidating lyase family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the copper type II
CC ascorbate-dependent monooxygenase family. {ECO:0000305}.
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DR EMBL; M19032; AAA49667.1; -; mRNA.
DR PIR; A27715; URXLA2.
DR RefSeq; NP_001081254.1; NM_001087785.1.
DR AlphaFoldDB; P12890; -.
DR SMR; P12890; -.
DR GeneID; 397736; -.
DR KEGG; xla:397736; -.
DR CTD; 397736; -.
DR Xenbase; XB-GENE-6252615; pam.S.
DR OrthoDB; 476471at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 397736; Expressed in heart and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
DR InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
DR InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR InterPro; IPR024548; Cu2_monoox_C.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000720; PHM/PAL.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR Pfam; PF01436; NHL; 3.
DR PRINTS; PR00790; PAMONOXGNASE.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR PROSITE; PS51125; NHL; 4.
PE 2: Evidence at transcript level;
KW Copper; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Lyase; Membrane;
KW Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..875
FT /note="Peptidyl-glycine alpha-amidating monooxygenase B"
FT /id="PRO_0000006368"
FT TOPO_DOM 40..763
FT /note="Intragranular"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 788..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 467..508
FT /note="NHL 1"
FT REPEAT 516..561
FT /note="NHL 2"
FT REPEAT 569..613
FT /note="NHL 3"
FT REPEAT 666..709
FT /note="NHL 4"
FT REGION 3..394
FT /note="Peptidylglycine alpha-hydroxylating monooxygenase"
FT /evidence="ECO:0000250"
FT REGION 395..716
FT /note="Peptidyl-alpha-hydroxyglycine alpha-amidating lyase"
FT /evidence="ECO:0000250"
FT REGION 735..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..184
FT /evidence="ECO:0000250"
FT DISULFID 79..124
FT /evidence="ECO:0000250"
FT DISULFID 112..129
FT /evidence="ECO:0000250"
FT DISULFID 225..332
FT /evidence="ECO:0000250"
FT DISULFID 291..313
FT /evidence="ECO:0000250"
FT DISULFID 530..551
FT /evidence="ECO:0000250"
FT DISULFID 598..609
FT /evidence="ECO:0000250"
SQ SEQUENCE 875 AA; 97085 MW; C07373AF6BF13450 CRC64;
MDMASLISSL LVLFLIFQNS CYCFRSPLSV FKRYEESTRS LSNDCLGTTR PVMSPGSSDY
TLDIRMPGVT PTESDTYLCK SYRLPVDDEA YVVDYRPHAN MDTAHHMLLF GCNVPSSTDD
YWDCSAGTCN DKSSIMYAWA KNAPPTKLPE GVGFQVGGKS GSRYFVLQVH YGDVKAFQDK
HKDCTGVTVR ITPEKQPLIA GIYLSMSLNT VVPPGQEVVN SDIACLYNRP TIHPFAYRVH
THQLGQVVSG FRVRHGKWTL IGRQSPQLPQ AFYPVEHPLE ISPGDIIATR CLFTGKGRMS
ATYIGGTAKD EMCNLYIMYY MDAAHATSYM TCVQTGNPKL FENIPEIANV PIPVSPDMMM
MMMMGHGHHH TEAEAETNTA LQQPKREEEE VLNQDVHLEE DTDWPGVNLK VGQVSGLALD
PKNNLVIFHR GDHVWDENSF DRNFVYQQRG IGPIQESTIL VVDPNTSKVL KSTGQNLFFL
PHGLTIDRDG NYWVTDVALH QVFKVGAEKE TPLLVLGRAF QPGSDRKHFC QPTDVAVDPI
TGNFFVADGY CNSRIMQFSP NGMFIMQWGE ETSSNLPRPG QFRIPHSLTM ISDQGQLCVA
DRENGRIQCF HAKTGEFVKQ IKHQEFGREV FAVSYAPGGV LYAVNGKPYY GDSTPVQGFM
LNFSNGDILD TFIPARKNFE MPHDIAAGDD GTVYVGDAHA NAVWKFSPSK AEHRSVKKAG
IEVEEITETE IFETHMRSRP KTNESVGQQT QEKPSVVQES SAGVSFVLII TLLIIPVVVL
IAIAIFIRWR KVRMYGGDIG HKSESSSGGI LGKLRGKGSG GLNLGTFFAT HKGYSRKGFD
RLSTEGSDQE KDDDDDGSDS EEEYSAPPIP PVSSS
