ID   NNMT_PIG                Reviewed;         264 AA.
AC   Q06AV1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Nicotinamide N-methyltransferase;
DE            EC=2.1.1.1;
GN   Name=NNMT;
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: Catalyzes the N-methylation of nicotinamide and other
CC       pyridines to form pyridinium ions. This activity is important for
CC       biotransformation of many drugs and xenobiotic compounds (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + nicotinamide = S-
CC       adenosyl-L-homocysteine + 1-methylnicotinamide.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NNMT/PNMT/TEMT family.
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DR   EMBL; DQ917624; ABI97169.1; -; mRNA.
DR   UniGene; Ssc.71079; -.
DR   SMR; Q06AV1; 1-260.
DR   HOVERGEN; Q06AV1; -.
DR   BRENDA; 2.1.1.1; 249.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008112; F:nicotinamide N-methyltransferase activity; IEA:EC.
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   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    264       Nicotinamide N-methyltransferase.
FT                                /FTId=PRO_0000262881.
FT   REGION       63     64       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      142    143       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   BINDING      20     20       S-adenosyl-L-methionine (By similarity).
FT   BINDING      25     25       S-adenosyl-L-methionine (By similarity).
FT   BINDING      69     69       S-adenosyl-L-methionine (By similarity).
FT   BINDING      85     85       S-adenosyl-L-methionine (By similarity).
FT   BINDING      90     90       S-adenosyl-L-methionine (By similarity).
FT   BINDING     163    163       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   264 AA;  29479 MW;  A9EC0A3A152E2BB4 CRC64;
     MESGFTSKDA YLSHFNPQDY LEKYYNFGAK HSAEDQILRH LLKILFKIFC LDGVKGDLLI
     DIGSGPTIYQ LLSACESFKE IIATDYTDQN LQELEKWLKK EPGAFDWSPV VTYVCELEGN
     RVKGTEKEEK LRRAVKRVLK CDVTQSWPLG AVPLPPADCL LSTLCLHAAC PDLPTYRTAL
     GNLRSLLKPG GFLVLVDALK SSYYMIGEQR FSSLCLGQEA VEAAVREAGY TIEHFEVISQ
     SYSSTMANNE GLFSLVGRKL SPCV
//