INMT_PONAB
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 03-AUG-2022, entry version 80.
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 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 OMA; CESFQDI; -.
DR OrthoDB; 1054662at2759; -.
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; -; 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 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
