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-MAR-2009, entry version 14.
DE   RecName: Full=Phenylethanolamine N-methyltransferase;
DE            Short=PNMTase;
DE            EC=2.1.1.28;
DE   AltName: Full=Noradrenaline N-methyltransferase;
GN   Name=PNMT;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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: Converts noradrenaline to adrenaline (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + phenylethanolamine =
CC       S-adenosyl-L-homocysteine + N-methylphenylethanolamine.
CC   -!- PATHWAY: Catecholamine biosynthesis; epinephrine biosynthesis;
CC       epinephrine from norepinephrine: step 1/1.
CC   -!- SIMILARITY: Belongs to the NNMT/PNMT/TEMT family.
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DR   EMBL; DQ917626; ABI97171.1; -; mRNA.
DR   RefSeq; NP_001116636.1; -.
DR   UniGene; Ssc.13910; -.
DR   SMR; Q06AU9; 14-279.
DR   GeneID; 100144479; -.
DR   KEGG; ssc:100144479; -.
DR   HOVERGEN; Q06AU9; -.
DR   BRENDA; 2.1.1.28; 249.
DR   GO; GO:0004603; F:phenylethanolamine N-methyltransferase acti...; IEA:EC.
DR   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000940; NNMT_TEMT_trans.
DR   PANTHER; PTHR10867; NNMT_TEMT_trans; 1.
DR   Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR   PIRSF; PIRSF000384; PNMTase; 1.
DR   PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
PE   2: Evidence at transcript level;
KW   Catecholamine biosynthesis; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    283       Phenylethanolamine N-methyltransferase.
FT                                /FTId=PRO_0000289662.
FT   REGION       79     80       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      158    159       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING      35     35       S-adenosyl-L-methionine (By similarity).
FT   BINDING      40     40       S-adenosyl-L-methionine (By similarity).
FT   BINDING      85     85       S-adenosyl-L-methionine (By similarity).
FT   BINDING     101    101       S-adenosyl-L-methionine (By similarity).
FT   BINDING     106    106       S-adenosyl-L-methionine (By similarity).
FT   BINDING     181    181       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     219    219       Substrate (By similarity).
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
//