ID   INMT_PONAB              Reviewed;         263 AA.
AC   Q5RFR7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Indolethylamine N-methyltransferase;
DE            Short=Indolamine N-methyltransferase;
DE            EC=2.1.1.49;
DE            EC=2.1.1.96;
DE   AltName: Full=Aromatic alkylamine N-methyltransferase;
DE            Short=Amine N-methyltransferase;
DE            Short=Arylamine N-methyltransferase;
DE   AltName: Full=Thioether S-methyltransferase;
GN   Name=INMT;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the N-methylation of tryptamine and structurally
CC       related compounds (By similarity). Functions as a thioether S-
CC       methyltransferase and is active with a variety of thioethers and the
CC       corresponding selenium and tellurium compounds, including 3-
CC       methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-
CC       methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and
CC       diethyl sulfide. Plays an important role in the detoxification of
CC       selenium compounds (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated
CC         tertiary amine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983;
CC         EC=2.1.1.49;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary amine + S-adenosyl-L-methionine = a methylated
CC         secondary amine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:53924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:137419, ChEBI:CHEBI:137984;
CC         EC=2.1.1.49;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary amine + S-adenosyl-L-methionine = a methylated
CC         primary amine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:23136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:65296, ChEBI:CHEBI:131823;
CC         EC=2.1.1.49;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethyl sulfide + S-adenosyl-L-methionine = S-adenosyl-L-
CC         homocysteine + trimethylsulfonium; Xref=Rhea:RHEA:19613,
CC         ChEBI:CHEBI:17434, ChEBI:CHEBI:17437, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789; EC=2.1.1.96;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; CR857085; CAH89390.1; -; mRNA.
DR   RefSeq; NP_001124586.1; NM_001131114.1.
DR   AlphaFoldDB; Q5RFR7; -.
DR   SMR; Q5RFR7; -.
DR   STRING; 9601.ENSPPYP00000019808; -.
DR   GeneID; 100171421; -.
DR   KEGG; pon:100171421; -.
DR   CTD; 11185; -.
DR   eggNOG; KOG4564; Eukaryota.
DR   HOGENOM; CLU_082526_2_0_1; -.
DR   InParanoid; Q5RFR7; -.
DR   OrthoDB; 5297821at2759; -.
DR   TreeFam; TF313114; -.
DR   Proteomes; UP000001595; Chromosome 7.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030748; F:amine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0102707; F:S-adenosyl-L-methionine:beta-alanine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004790; F:thioether S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
DR   GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
DR   InterPro; IPR000940; NNMT_TEMT_trans.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; NF041360; GntF_guanitoxin; 1.
DR   PANTHER; PTHR10867:SF33; INDOLETHYLAMINE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10867; NNMT/PNMT/TEMT FAMILY MEMBER; 1.
DR   Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR   PIRSF; PIRSF000384; PNMTase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
DR   PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Detoxification; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..263
FT                   /note="Indolethylamine N-methyltransferase"
FT                   /id="PRO_0000159714"
FT   BINDING         20
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         13
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P40936"
FT   MOD_RES         96
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P40936"
SQ   SEQUENCE   263 AA;  28848 MW;  05387543210CB66B CRC64;
     MEGGFTGGDE YQKHFLPRDY LATYYSFDGS PSPEAEMLKF NLECLHKTFG PGGLQGDTLI
     DIGSGPTIYQ VLAACESFQD ITLSDFTDRN REELEKWLKK EPGAYDWTPV VKFACELEGN
     SGQWEEKEEK LRATVKRVLK CDVHLGNPLA PAVLPPADCV LTLLAMECAC CSLDAYCAAL
     CNLASLLKPG GHLVTTVTLR LSSYMVGKRE FSCVALEKEE VEQAVLDAGF DIEQLLQSPQ
     SYSVTNAANN GVCFIVARKK PGP
//