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}.
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; 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
//
