NNMT1_CAEEL
ID NNMT1_CAEEL Reviewed; 273 AA.
AC P34254;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nicotinamide N-methyltransferase {ECO:0000250|UniProtKB:P40261};
DE EC=2.1.1.1 {ECO:0000250|UniProtKB:P40261};
GN Name=anmt-1 {ECO:0000312|WormBase:B0303.2};
GN ORFNames=B0303.2 {ECO:0000312|WormBase:B0303.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1538779; DOI=10.1038/356037a0;
RA Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA Waterston R.;
RT "The C. elegans genome sequencing project: a beginning.";
RL Nature 356:37-41(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24077178; DOI=10.1038/nchembio.1352;
RA Schmeisser K., Mansfeld J., Kuhlow D., Weimer S., Priebe S., Heiland I.,
RA Birringer M., Groth M., Segref A., Kanfi Y., Price N.L., Schmeisser S.,
RA Schuster S., Pfeiffer A.F., Guthke R., Platzer M., Hoppe T., Cohen H.Y.,
RA Zarse K., Sinclair D.A., Ristow M.;
RT "Role of sirtuins in lifespan regulation is linked to methylation of
RT nicotinamide.";
RL Nat. Chem. Biol. 9:693-700(2013).
CC -!- FUNCTION: Catalyzes the N-methylation of nicotinamide and other
CC pyridines to form pyridinium ions (By similarity). Involved in
CC regulation of lifespan extension downstream of the sirtuin sir-2.1,
CC probably through its role in nicotinic acid metabolism
CC (PubMed:24077178). {ECO:0000250|UniProtKB:P40261,
CC ECO:0000269|PubMed:24077178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nicotinamide + S-adenosyl-L-methionine = 1-methylnicotinamide
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23884, ChEBI:CHEBI:16797,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:P40261};
CC -!- DISRUPTION PHENOTYPE: Suppressed lifespan extension when exposed to
CC nicotinic acid and nicotinamide. Reduced reactive oxygen species levels
CC when exposed to nicotinic acid. {ECO:0000269|PubMed:24077178}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. NNMT/PNMT/TEMT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO080163; CCD61707.1; -; Genomic_DNA.
DR PIR; S27784; S27784.
DR RefSeq; NP_498914.1; NM_066513.4.
DR AlphaFoldDB; P34254; -.
DR SMR; P34254; -.
DR BioGRID; 41420; 2.
DR STRING; 6239.B0303.2; -.
DR EPD; P34254; -.
DR PaxDb; P34254; -.
DR PeptideAtlas; P34254; -.
DR EnsemblMetazoa; B0303.2.1; B0303.2.1; WBGene00015124.
DR EnsemblMetazoa; B0303.2.2; B0303.2.2; WBGene00015124.
DR GeneID; 176217; -.
DR KEGG; cel:CELE_B0303.2; -.
DR UCSC; B0303.2; c. elegans.
DR CTD; 176217; -.
DR WormBase; B0303.2; CE00536; WBGene00015124; anmt-1.
DR eggNOG; ENOG502RY9W; Eukaryota.
DR GeneTree; ENSGT00390000011708; -.
DR HOGENOM; CLU_082526_0_0_1; -.
DR InParanoid; P34254; -.
DR OMA; CLEYSCE; -.
DR OrthoDB; 1054662at2759; -.
DR PhylomeDB; P34254; -.
DR BRENDA; 2.1.1.1; 1045.
DR Reactome; R-CEL-156581; Methylation.
DR Reactome; R-CEL-197264; Nicotinamide salvaging.
DR Reactome; R-CEL-209905; Catecholamine biosynthesis.
DR PRO; PR:P34254; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015124; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0005863; C:striated muscle myosin thick filament; HDA:WormBase.
DR GO; GO:0008170; F:N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008112; F:nicotinamide N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
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; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..273
FT /note="Nicotinamide N-methyltransferase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000159716"
FT BINDING 35
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P40261"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P40261"
FT BINDING 74..75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P40261"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P40261"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P40261"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P40261"
FT BINDING 152..153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P40261"
SQ SEQUENCE 273 AA; 30860 MW; 11A793EC49C270C0 CRC64;
MTGTTENDNT GEDEKPKDEE CAAIEHKDKF NPTAYLNSFY KTASEDTAMQ IVLFFLPGIL
YRLPQKVRSV LDLGAGPTVY LPISLRDRAE NIYTSDYAPA NRDTLINWIE DKSDFDWDNV
CSWIANIEAS METGKQMQNK TRKLMRAVLD VNVHESPVVQ SIVWKENEQV QVPDKFQVVS
TVFCLEYSCE TLEAYFRAVR SACSLIDEGG ILIQGGVLDA TTYNFGGKTF RCHRLKQAHI
IESLKANGMA TTAEQGYKFI THDDIFLLVS KKL
