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 16-JUN-2009, entry version 18. DE RecName: Full=Histamine N-methyltransferase; DE Short=HMT; DE EC=2.1.1.8; GN Name=hnmt; ORFNames=GSTENG00020755001; OS Tetraodon nigroviridis (Green puffer). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC 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., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). CC -!- FUNCTION: Inactivates histamine by N-methylation. Plays an CC important role in degrading histamine and in regulating the airway CC response to histamine (By similarity). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histamine = S- CC adenosyl-L-homocysteine + N(tau)-methylhistamine. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HNMT CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAE01014661; CAG01846.1; -; Genomic_DNA. DR NMPDR; fig|99883.3.peg.15722; -. DR HOVERGEN; Q4SBY6; -. DR OMA; Q4SBY6; YDLLSTM. DR BRENDA; 2.1.1.8; 295302. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046539; F:histamine N-methyltransferase activity; IEA:EC. DR InterPro; IPR016673; Histamine_N-methyltransferase. DR PIRSF; PIRSF016616; HHMT; 1. PE 3: Inferred from homology; KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 291 Histamine N-methyltransferase. FT /FTId=PRO_0000271425. FT BINDING 28 28 Substrate (By similarity). FT BINDING 60 60 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT BINDING 89 89 S-adenosyl-L-methionine (By similarity). FT BINDING 94 94 S-adenosyl-L-methionine (By similarity). FT BINDING 142 142 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT BINDING 283 283 Substrate (By similarity). 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 //