PNMT_PIG
ID PNMT_PIG Reviewed; 283 AA.
AC Q06AU9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Phenylethanolamine N-methyltransferase;
DE Short=PNMTase;
DE EC=2.1.1.28 {ECO:0000250|UniProtKB:P11086};
DE AltName: Full=Noradrenaline N-methyltransferase;
GN Name=PNMT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transmethylation of nonepinephrine
CC (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-
CC methionine as the methyl donor. Other substrates include
CC phenylethanolamine, octopamine and normetanephrine (By similarity).
CC {ECO:0000250|UniProtKB:P11086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phenylethanolamine + S-adenosyl-L-methionine = H(+) + N-
CC methylphenylethanolamine + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:12176, ChEBI:CHEBI:15378, ChEBI:CHEBI:57741,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:57946, ChEBI:CHEBI:59789; EC=2.1.1.28;
CC Evidence={ECO:0000250|UniProtKB:P11086};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12177;
CC Evidence={ECO:0000250|UniProtKB:P11086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-noradrenaline + S-adenosyl-L-methionine = (R)-adrenaline +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:25269,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:71406, ChEBI:CHEBI:72587; EC=2.1.1.28;
CC Evidence={ECO:0000250|UniProtKB:P11086};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25270;
CC Evidence={ECO:0000250|UniProtKB:P11086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-normetanephrine + S-adenosyl-L-methionine = H(+) + N-
CC methyl-(R)-normetanephrine + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70683, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:189645, ChEBI:CHEBI:189646;
CC Evidence={ECO:0000250|UniProtKB:P10937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70684;
CC Evidence={ECO:0000250|UniProtKB:P10937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-octopamine + S-adenosyl-L-methionine = (R)-synephrine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70519,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:63694, ChEBI:CHEBI:141486;
CC Evidence={ECO:0000250|UniProtKB:P10937};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70520;
CC Evidence={ECO:0000250|UniProtKB:P10937};
CC -!- PATHWAY: Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-
CC adrenaline from (R)-noradrenaline: step 1/1.
CC {ECO:0000250|UniProtKB:P11086}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. NNMT/PNMT/TEMT family. {ECO:0000305}.
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DR EMBL; DQ917626; ABI97171.1; -; mRNA.
DR RefSeq; NP_001116636.1; NM_001123164.1.
DR AlphaFoldDB; Q06AU9; -.
DR SMR; Q06AU9; -.
DR STRING; 9823.ENSSSCP00000018549; -.
DR PaxDb; Q06AU9; -.
DR PRIDE; Q06AU9; -.
DR Ensembl; ENSSSCT00000019054; ENSSSCP00000018549; ENSSSCG00000017501.
DR Ensembl; ENSSSCT00025078014; ENSSSCP00025033812; ENSSSCG00025057035.
DR Ensembl; ENSSSCT00035075914; ENSSSCP00035030955; ENSSSCG00035056795.
DR Ensembl; ENSSSCT00045065783; ENSSSCP00045046575; ENSSSCG00045038036.
DR Ensembl; ENSSSCT00050092630; ENSSSCP00050039929; ENSSSCG00050067889.
DR Ensembl; ENSSSCT00055007324; ENSSSCP00055005785; ENSSSCG00055003728.
DR Ensembl; ENSSSCT00065103151; ENSSSCP00065045556; ENSSSCG00065074846.
DR Ensembl; ENSSSCT00070033324; ENSSSCP00070027835; ENSSSCG00070016924.
DR GeneID; 100144479; -.
DR KEGG; ssc:100144479; -.
DR CTD; 5409; -.
DR VGNC; VGNC:91602; PNMT.
DR eggNOG; ENOG502QT44; Eukaryota.
DR GeneTree; ENSGT00390000011708; -.
DR HOGENOM; CLU_082526_2_0_1; -.
DR InParanoid; Q06AU9; -.
DR OMA; IDVHCSQ; -.
DR OrthoDB; 1054662at2759; -.
DR TreeFam; TF313114; -.
DR Reactome; R-SSC-209905; Catecholamine biosynthesis.
DR UniPathway; UPA00749; UER00736.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Chromosome 12.
DR Bgee; ENSSSCG00000017501; Expressed in longissimus lumborum muscle and 12 other tissues.
DR ExpressionAtlas; Q06AU9; differential.
DR Genevisible; Q06AU9; SS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008170; F:N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0004603; F:phenylethanolamine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042418; P:epinephrine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
DR InterPro; IPR000940; NNMT_TEMT_trans.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10867; PTHR10867; 1.
DR Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR PIRSF; PIRSF000384; PNMTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
DR PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
PE 2: Evidence at transcript level;
KW Catecholamine biosynthesis; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT CHAIN 2..283
FT /note="Phenylethanolamine N-methyltransferase"
FT /id="PRO_0000289662"
FT BINDING 35
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 79..80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 158..159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 219
FT /ligand="octopamine"
FT /ligand_id="ChEBI:CHEBI:58025"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT BINDING 267
FT /ligand="octopamine"
FT /ligand_id="ChEBI:CHEBI:58025"
FT /evidence="ECO:0000250|UniProtKB:P11086"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11086"
SQ SEQUENCE 283 AA; 30879 MW; 15ADE065A8F4B8C4 CRC64;
MSGTGQSHAA DAAPDSDPGQ AAVALAYQHF EPRAYLRNNY APPRGDLSSP DGVGPWKLRC
LAQTFATGEV SGRALIDIGS GPTIYQLLSA CAHFEDITMT DFLEVNRQEL GLWLREEPGA
FDWSVYSQHV CLIEGKGESC QEKERQLRAR VKRILPIDVH QPQPLGTGSL APLPADALVS
AFCLEAVSPD LASFQRALDH ITTLLRSGGH LLLIGALEES WYLAGEARLA VVPVCEEEVR
EALARSGYEV RDLRTYVMPA HLRTGVDDVK GIFFAWAQKK VGV
