ID HNMT_DANRE Reviewed; 292 AA. AC Q6DC37; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 04-NOV-2026, entry version 94. DE RecName: Full=Histamine N-methyltransferase; DE Short=HMT; DE EC=2.1.1.8 {ECO:0000250|UniProtKB:P50135}; GN Name=hnmt; ORFNames=zgc:100917; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. 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 = N(tele)-methylhistamine CC + S-adenosyl-L-homocysteine + H(+); 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; BC078250; AAH78250.1; -; mRNA. DR RefSeq; NP_001003636.1; NM_001003636.2. DR RefSeq; NP_001428663.1; NM_001441734.1. DR AlphaFoldDB; Q6DC37; -. DR SMR; Q6DC37; -. DR FunCoup; Q6DC37; 897. DR STRING; 7955.ENSDARP00000113843; -. DR PaxDb; 7955-ENSDARP00000113843; -. DR PeptideAtlas; Q6DC37; -. DR GeneID; 445242; -. DR AGR; ZFIN:ZDB-GENE-040801-157; -. DR CTD; 3176; -. DR ZFIN; ZDB-GENE-040801-157; hnmt. DR eggNOG; ENOG502QQJ1; Eukaryota. DR InParanoid; Q6DC37; -. DR OrthoDB; 5984880at2759; -. DR PhylomeDB; Q6DC37; -. DR PRO; PR:Q6DC37; -. DR Proteomes; UP000000437; Chromosome 9. 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 FunFam; 3.40.50.150:FF:000118; Histamine N-methyltransferase; 1. 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 2: Evidence at transcript level; KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1..292 FT /note="Histamine N-methyltransferase" FT /id="PRO_0000271424" 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 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 292 AA; 33619 MW; E95CBB203B845FBD CRC64; MAAPFKTLVE DYPRYLKSFE LFLERSSEHQ CMQDFIHNTL PDILASIGGG RSVFNVMGVG SGAGDIDLEM LAQLHLKHPH VKVDNEVVEP SNDMLYKYKA RVSTSPDLAY INFTWNKMTA SEFEKQWQEK TPEKKMDFIH MIQMLYYVKD PNATVSFFRS LLEKDGKLLI ILVSGESGWG KLWTTFRKQL CYTEMSQCVT IGEIKSFLDS EGVPYRKYVL LSQMDITECF TEGDQEGELL LDFLTEVKEF SKNAPERLKK EVLDVLRHPD CSKEVDGRII FNNNLEVLVI EP //