ID C3Y6T8_BRAFL Unreviewed; 163 AA.
AC C3Y6T8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Serotonin N-acetyltransferase {ECO:0000256|ARBA:ARBA00039398};
DE EC=2.3.1.87 {ECO:0000256|ARBA:ARBA00039114};
DE AltName: Full=Aralkylamine N-acetyltransferase {ECO:0000256|ARBA:ARBA00042928};
GN ORFNames=BRAFLDRAFT_74988 {ECO:0000313|EMBL:EEN64048.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN64048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN64048.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN64048.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine
CC + CoA + H(+); Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:77827; EC=2.3.1.87;
CC Evidence={ECO:0000256|ARBA:ARBA00036561};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000256|ARBA:ARBA00037926}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily.
CC {ECO:0000256|ARBA:ARBA00038182}.
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DR EMBL; GG666488; EEN64048.1; -; Genomic_DNA.
DR RefSeq; XP_002608038.1; XM_002607992.1.
DR AlphaFoldDB; C3Y6T8; -.
DR STRING; 7739.C3Y6T8; -.
DR eggNOG; KOG4144; Eukaryota.
DR InParanoid; C3Y6T8; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0030187; P:melatonin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR10908; SEROTONIN N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10908:SF0; SEROTONIN N-ACETYLTRANSFERASE; 1.
DR Pfam; PF13673; Acetyltransf_10; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Melatonin biosynthesis {ECO:0000256|ARBA:ARBA00043260};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..163
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 163 AA; 18109 MW; 8B9B8B0213B3A153 CRC64;
MAEGNVRPLQ CGEEVEQASI LESAGYPADE AASLETLQAR HTAESRLFIG YFENEKLLGF
VCATSTDADR LTEESMHTHI PHGETICIHS VCVDQSVQRQ GIATKLLKEF VHNVKGSFPD
AKRICLICHE YLIPLYTKAG FVLVGLSEVV HGKEPWYDCV MEL
//
