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   03-AUG-2022, entry version 83.
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 = 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; BC078250; AAH78250.1; -; mRNA.
DR   RefSeq; NP_001003636.1; NM_001003636.1.
DR   AlphaFoldDB; Q6DC37; -.
DR   SMR; Q6DC37; -.
DR   STRING; 7955.ENSDARP00000113843; -.
DR   PaxDb; Q6DC37; -.
DR   GeneID; 445242; -.
DR   KEGG; dre:445242; -.
DR   CTD; 3176; -.
DR   ZFIN; ZDB-GENE-040801-157; hnmt.
DR   eggNOG; ENOG502QQJ1; Eukaryota.
DR   InParanoid; Q6DC37; -.
DR   OrthoDB; 870728at2759; -.
DR   PhylomeDB; Q6DC37; -.
DR   PRO; PR:Q6DC37; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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; -; 1.
DR   InterPro; IPR016673; HHMT-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PIRSF; PIRSF016616; HHMT; 1.
DR   SUPFAM; SSF53335; SSF53335; 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