ID   HNMT_TETNG              Reviewed;         291 AA.
AC   Q4SBY6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   22-FEB-2023, entry version 61.
DE   RecName: Full=Histamine N-methyltransferase;
DE            Short=HMT;
DE            EC=2.1.1.8 {ECO:0000250|UniProtKB:P50135};
GN   Name=hnmt; ORFNames=GSTENG00020755001;
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
CC   -!- FUNCTION: Inactivates histamine by N-methylation. Plays an important
CC       role in degrading histamine and in regulating the airway response to
CC       histamine. {ECO:0000250|UniProtKB:P50135}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=histamine + S-adenosyl-L-methionine = H(+) + N(tau)-
CC         methylhistamine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19301,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58432,
CC         ChEBI:CHEBI:58600, ChEBI:CHEBI:59789; EC=2.1.1.8;
CC         Evidence={ECO:0000250|UniProtKB:P50135, ECO:0000255|PROSITE-
CC         ProRule:PRU00929};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P50135}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50135}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. HNMT family. {ECO:0000255|PROSITE-ProRule:PRU00929}.
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DR   EMBL; CAAE01014661; CAG01846.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4SBY6; -.
DR   SMR; Q4SBY6; -.
DR   STRING; 99883.ENSTNIP00000013918; -.
DR   KEGG; tng:GSTEN00020755G001; -.
DR   HOGENOM; CLU_058117_1_0_1; -.
DR   InParanoid; Q4SBY6; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0046539; F:histamine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0001695; P:histamine catabolic process; ISS:UniProtKB.
DR   GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR016673; HHMT-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   PIRSF; PIRSF016616; HHMT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51597; SAM_HNMT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..291
FT                   /note="Histamine N-methyltransferase"
FT                   /id="PRO_0000271425"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT   BINDING         60
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT   BINDING         89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
SQ   SEQUENCE   291 AA;  32938 MW;  8550AE3B0DA4ADB1 CRC64;
     MASAMRSLIE DDSRYLKSFK LFLERSTEHQ CVQEFIHNVL PDILGSVGKG KTHLNVIGVG
     SGAGEVDLEI LSELHSRHPG ASVDNEVVEP SAQQLQDYKA LVLQKKDLDY ISFNWNKMTA
     TEFEERWRAN KMSKEADFIH MIQMLYYVKD PEATTSFFQS LLSKTGKLLI ILVSGNSGWG
     KLWKTYKNQF CNPEISQCVT TADIQSFLDS KGARYQSFEL PSQMDITECF TQGDEKGELL
     LDFLTEVLEF SKTASPELRA EVMELLRHPD CSVESNGRVM FNNNLGVIVL D
//