ASMT_BOVIN
ID ASMT_BOVIN Reviewed; 345 AA.
AC P10950; Q28123;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 116.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Pineal gland;
RX PubMed=3818627; DOI=10.1016/s0021-9258(18)61591-1;
RA Ishida I., Obinata M., Deguchi T.;
RT "Molecular cloning and nucleotide sequence of cDNA encoding hydroxyindole
RT O-methyltransferase of bovine pineal glands.";
RL J. Biol. Chem. 262:2895-2899(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
RX PubMed=1544900; DOI=10.1016/s0021-9258(18)42748-2;
RA Donohue S.J., Roseboom P.H., Klein D.C.;
RT "Bovine hydroxyindole-O-methyltransferase. Significant sequence revision.";
RL J. Biol. Chem. 267:5184-5185(1992).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=8574683; DOI=10.1016/0006-8993(95)00651-6;
RA Bernard M., Donohue S.J., Klein D.C.;
RT "Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79
RT retinoblastoma cells.";
RL Brain Res. 696:37-48(1995).
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: Expressed in the pineal gland (at protein level).
CC Not detectable in retina, nor in liver. {ECO:0000269|PubMed:3818627,
CC ECO:0000269|PubMed:8574683}.
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; J02671; AAA30565.1; -; mRNA.
DR EMBL; M81862; AAA30570.1; -; mRNA.
DR PIR; A42106; A42106.
DR RefSeq; NP_803459.1; NM_177493.2.
DR AlphaFoldDB; P10950; -.
DR SMR; P10950; -.
DR STRING; 9913.ENSBTAP00000054648; -.
DR ChEMBL; CHEMBL3243914; -.
DR PaxDb; P10950; -.
DR Ensembl; ENSBTAT00000067824; ENSBTAP00000064490; ENSBTAG00000049541.
DR GeneID; 281013; -.
DR KEGG; bta:281013; -.
DR CTD; 438; -.
DR VEuPathDB; HostDB:ENSBTAG00000049541; -.
DR eggNOG; KOG3178; Eukaryota.
DR GeneTree; ENSGT00940000161561; -.
DR InParanoid; P10950; -.
DR OMA; EYMEGFL; -.
DR OrthoDB; 817726at2759; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000049541; Expressed in biceps femoris and 79 other tissues.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
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 1: Evidence at protein 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_0000083980"
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"
FT CONFLICT 18
FT /note="G -> A (in Ref. 1; AAA30565)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..121
FT /note="QGTELLLNTCVSLKLLQADVRGGKAVYANTELASTYLVRGSPRSQRDMLLYA
FT GRTAYVCWRHLA -> GDRAATEHLCVPEAAASRREGRKSCVCKHGARQHLPGERQPQV
FT PAGHAAVRGQDRLRLLAPPG (in Ref. 1; AAA30565)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..345
FT /note="AEYRALLGPAGFRDVRCRRTGGTYDAVLARK -> GRSTARSVGPAASETCG
FT DGGRGEPTMLSWPGNQACSV (in Ref. 1; AAA30565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 37924 MW; AA8EB84EB8D4A7E4 CRC64;
MCSQEGEGYS LLKEYANGFM VSQVLFAACE LGVFELLAEA LEPLDSAAVS SHLGSSPQGT
ELLLNTCVSL KLLQADVRGG KAVYANTELA STYLVRGSPR SQRDMLLYAG RTAYVCWRHL
AEAVREGRNQ YLKAFGIPSE ELFSAIYRSE DERLQFMQGL QDVWRLEGAT VLAAFDLSPF
PLICDLGGGS GALAKACVSL YPGCRAIVFD IPGVVQIAKR HFSASEDERI SFHEGDFFKD
ALPEADLYIL ARVLHDWTDA KCSHLLQRVY RACRTGGGIL VIESLLDTDG RGPLTTLLYS
LNMLVQTEGR ERTPAEYRAL LGPAGFRDVR CRRTGGTYDA VLARK
