ID   HNMT_XENTR              Reviewed;         293 AA.
AC   Q0V9P1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, 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;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; BC121451; AAI21452.1; -; mRNA.
DR   RefSeq; NP_001072355.1; -.
DR   UniGene; Str.53540; -.
DR   GeneID; 779808; -.
DR   KEGG; xtr:779808; -.
DR   Xenbase; XB-FEAT-1001068; hnmt.
DR   HOVERGEN; Q0V9P1; -.
DR   BRENDA; 2.1.1.8; 279072.
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   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    293       Histamine N-methyltransferase.
FT                                /FTId=PRO_0000271428.
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     120    120       S-adenosyl-L-methionine; via amide
FT                                nitrogen (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   293 AA;  33115 MW;  29F7F721066A09BB CRC64;
     MDSGLRSLLS DHSRYVESFR LFLLNSTEHQ CMQRFIDTQF PHIVSSIGKD KSVIDILGIG
     SGSGEIDLQM IGKIQSRHPG VAISNQIVEP SAEQIIGYKE RVAKAPNLGA VSFSWHRQTS
     SEYERQVNEE KQMRSYDFIH MIQMLYYVKD VPATLRFFKS CLAPNGKLLI ILVSGNSGWS
     MLWKKHGPQL PLNDLCLYVT AGDIAQMLSS MGARFQSYEL PSDMDITECF IEGDRNGEML
     LDFLTETCDF KRNAPADLRE QILCDLKSPE CSTTRDGKVI FNNNLSVIVV ERD
//