ASMT_MACMU
ID ASMT_MACMU Reviewed; 345 AA.
AC Q8HZJ0;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Acetylserotonin O-methyltransferase;
DE EC=2.1.1.4 {ECO:0000250|UniProtKB:B3GSH5};
DE AltName: Full=Hydroxyindole O-methyltransferase;
DE Short=HIOMT;
GN Name=ASMT;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Pineal gland;
RX PubMed=12364461; DOI=10.1210/jc.2002-020683;
RA Coon S.L., Del Olmo E., Young W.S. III, Klein D.C.;
RT "Melatonin synthesis enzymes in Macaca mulatta: focus on arylalkylamine N-
RT acetyltransferase (EC 2.3.1.87).";
RL J. Clin. Endocrinol. Metab. 87:4699-4706(2002).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group onto N-
CC acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
CC {ECO:0000250|UniProtKB:B3GSH5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15573, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16796, ChEBI:CHEBI:17697, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:B3GSH5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15574;
CC Evidence={ECO:0000250|UniProtKB:B3GSH5};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000250|UniProtKB:B3GSH5}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pineal gland. In the retina,
CC 10- to 100-fold lower expression compared to pineal gland, if any.
CC {ECO:0000269|PubMed:12364461}.
CC -!- INDUCTION: No night/day variations. {ECO:0000269|PubMed:12364461}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AY069924; AAL49966.1; -; mRNA.
DR RefSeq; NP_001028112.1; NM_001032940.1.
DR AlphaFoldDB; Q8HZJ0; -.
DR SMR; Q8HZJ0; -.
DR STRING; 9544.ENSMMUP00000038234; -.
DR GeneID; 574350; -.
DR KEGG; mcc:574350; -.
DR CTD; 438; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_1953717_0_0_1; -.
DR InParanoid; Q8HZJ0; -.
DR OrthoDB; 817726at2759; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030187; P:melatonin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031725; ASMT_dimerisation.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF16864; Dimerisation2; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 2: Evidence at transcript level;
KW Lipid metabolism; Melatonin biosynthesis; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..345
FT /note="Acetylserotonin O-methyltransferase"
FT /id="PRO_0000083983"
FT ACT_SITE 255
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 235..237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 38160 MW; B7DD9CE4625C0FF7 CRC64;
MGSSGDDGYR LLNEYTNGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVEASSHGT
ELLLDTCVSL KLLKVETRAG KAFYQNTELS SAYLTRVSPT SQCNLLKYMG RTSYGCWGHL
ADAVREGKNQ YLQTFGVPAE DLFKAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSGF
PLMCDLGGGP GALAKECLSL YPGCKVTVFD VPEVVRTAKQ HFSFPEEEEI HLQEGDFFKD
PLPEADLYIL ARILHDWADG KCSHLLERVY HTCKPGGGIL VIESLLDEDR RGPLLTQLYS
LNMLVQTEGQ ERTPTHYHML LSSAGFRDFQ FKKTGAIYDA ILVRK
