ASMT_CHICK
ID ASMT_CHICK Reviewed; 346 AA.
AC Q92056;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Acetylserotonin O-methyltransferase;
DE EC=2.1.1.4 {ECO:0000269|PubMed:1372168};
DE AltName: Full=Hydroxyindole O-methyltransferase;
DE Short=HIOMT;
GN Name=ASMT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
RC STRAIN=Hubbard; TISSUE=Pineal gland;
RX PubMed=1372168; DOI=10.1042/bj2820571;
RA Voisin P., Guerlotte J., Bernard M., Collin J.P., Cogne M.;
RT "Molecular cloning and nucleotide sequence of a cDNA encoding hydroxyindole
RT O-methyltransferase from chicken pineal gland.";
RL Biochem. J. 282:571-576(1992).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group onto N-
CC acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
CC {ECO:0000269|PubMed:1372168}.
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; Evidence={ECO:0000269|PubMed:1372168};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15574;
CC Evidence={ECO:0000305|PubMed:1372168};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for N-acetylserotonin {ECO:0000269|PubMed:1372168};
CC KM=8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:1372168};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000305|PubMed:1372168}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in pineal gland and retina.
CC {ECO:0000269|PubMed:1372168}.
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; X62309; CAA44189.1; -; mRNA.
DR PIR; S21265; S21265.
DR RefSeq; NP_990674.1; NM_205343.1.
DR AlphaFoldDB; Q92056; -.
DR SMR; Q92056; -.
DR STRING; 9031.ENSGALP00000026872; -.
DR PaxDb; Q92056; -.
DR GeneID; 396286; -.
DR KEGG; gga:396286; -.
DR CTD; 438; -.
DR VEuPathDB; HostDB:geneid_396286; -.
DR eggNOG; KOG3178; Eukaryota.
DR InParanoid; Q92056; -.
DR OrthoDB; 817726at2759; -.
DR PhylomeDB; Q92056; -.
DR UniPathway; UPA00837; UER00815.
DR PRO; PR:Q92056; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
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..346
FT /note="Acetylserotonin O-methyltransferase"
FT /id="PRO_0000083981"
FT ACT_SITE 256
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 236..238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 39136 MW; 3EB370E4488CC5E8 CRC64;
MDSTEDLDYP QIIFQYSNGF LVSKVMFTAC ELGVFDLLLQ SGRPLSLDVI AARLGTSIMG
MERLLDACVG LKLLAVELRR EGAFYRNTEI SNIYLTKSSP KSQYHIMMYY SNTVYLCWHY
LTDAVREGRN QYERAFGISS KDLFGARYRS EEEMLKFLAG QNSIWSICGR DVLTAFDLSP
FTQIYDLGGG GGALAQECVF LYPNCTVTIY DLPKVVQVAK ERLVPPEERR IAFHEGDFFK
DSIPEADLYI LSKILHDWDD KKCRQLLAEV YKACRPGGGV LLVESLLSED RSGPVETQLY
SLNMLVQTEG KERTAVEYSE LLGAAGFREV QVRRTGKLYD AVLGRK
