ID   SNAT2_ORYSJ             Reviewed;         200 AA.
AC   Q6Z1Y6;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Serotonin N-acetyltransferase 2, chloroplastic {ECO:0000303|PubMed:27121038};
DE            Short=OsSNAT2 {ECO:0000303|PubMed:27121038};
DE            EC=2.3.1.87 {ECO:0000269|PubMed:27121038};
DE   Flags: Precursor;
GN   Name=SNAT2 {ECO:0000303|PubMed:27121038};
GN   OrderedLocusNames=Os08g0102000 {ECO:0000312|EMBL:BAT03408.1},
GN   LOC_Os08g01170 {ECO:0000305};
GN   ORFNames=B1147B12.22 {ECO:0000312|EMBL:BAD03558.1},
GN   OsJ_25726 {ECO:0000312|EMBL:EAZ41221.1},
GN   P0015C07.5 {ECO:0000312|EMBL:BAD33154.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND INDUCTION.
RX   PubMed=27121038; DOI=10.1111/jpi.12339;
RA   Byeon Y., Lee H.Y., Back K.;
RT   "Cloning and characterization of the serotonin N-acetyltransferase-2 gene
RT   (SNAT2) in rice (Oryza sativa).";
RL   J. Pineal Res. 61:198-207(2016).
CC   -!- FUNCTION: Catalyzes the N-acetylation of serotonin into N-
CC       acetylserotonin, the penultimate step in the synthesis of melatonin
CC       (PubMed:27121038). Catalyzes in vitro the N-acetylation of tryptamine
CC       to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin
CC       and tyramine to produce N-acetyltyramine (PubMed:27121038).
CC       {ECO:0000269|PubMed:27121038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + serotonin = CoA + H(+) + N-acetylserotonin;
CC         Xref=Rhea:RHEA:25217, ChEBI:CHEBI:15378, ChEBI:CHEBI:17697,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:350546;
CC         EC=2.3.1.87; Evidence={ECO:0000269|PubMed:27121038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25218;
CC         Evidence={ECO:0000269|PubMed:27121038};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + tyramine = CoA + H(+) + N-acetyltyramine;
CC         Xref=Rhea:RHEA:66136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:125610, ChEBI:CHEBI:327995;
CC         Evidence={ECO:0000269|PubMed:27121038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66137;
CC         Evidence={ECO:0000269|PubMed:27121038};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + tryptamine = CoA + H(+) + N-acetyltryptamine;
CC         Xref=Rhea:RHEA:66196, ChEBI:CHEBI:15378, ChEBI:CHEBI:55515,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57887;
CC         Evidence={ECO:0000269|PubMed:27121038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66197;
CC         Evidence={ECO:0000269|PubMed:27121038};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methoxytryptamine + acetyl-CoA = CoA + H(+) + melatonin;
CC         Xref=Rhea:RHEA:66144, ChEBI:CHEBI:15378, ChEBI:CHEBI:16796,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:166874;
CC         Evidence={ECO:0000269|PubMed:27121038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66145;
CC         Evidence={ECO:0000269|PubMed:27121038};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=371 uM for serotonin {ECO:0000269|PubMed:27121038};
CC         Vmax=4.7 nmol/min/mg enzyme with serotonin as substrate
CC         {ECO:0000269|PubMed:27121038};
CC       pH dependence:
CC         Optimum pH is 8.8. {ECO:0000269|PubMed:27121038};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:27121038};
CC   -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC       melatonin from serotonin: step 1/2. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27121038}. Plastid,
CC       chloroplast {ECO:0000269|PubMed:27121038}.
CC   -!- INDUCTION: Down-regulated by cadmium. {ECO:0000269|PubMed:27121038}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP004654; BAD33154.1; -; Genomic_DNA.
DR   EMBL; AP005406; BAD03558.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF22679.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT03408.1; -; Genomic_DNA.
DR   EMBL; CM000145; EAZ41221.1; -; Genomic_DNA.
DR   EMBL; AK068156; BAG90782.1; -; mRNA.
DR   RefSeq; XP_015648698.1; XM_015793212.1.
DR   AlphaFoldDB; Q6Z1Y6; -.
DR   SMR; Q6Z1Y6; -.
DR   STRING; 4530.OS08T0102000-01; -.
DR   PaxDb; Q6Z1Y6; -.
DR   PRIDE; Q6Z1Y6; -.
DR   EnsemblPlants; Os08t0102000-01; Os08t0102000-01; Os08g0102000.
DR   GeneID; 4344423; -.
DR   Gramene; Os08t0102000-01; Os08t0102000-01; Os08g0102000.
DR   KEGG; osa:4344423; -.
DR   eggNOG; ENOG502RZ2D; Eukaryota.
DR   HOGENOM; CLU_086503_0_2_1; -.
DR   InParanoid; Q6Z1Y6; -.
DR   OMA; FARCTGD; -.
DR   OrthoDB; 1429454at2759; -.
DR   BRENDA; 2.3.1.87; 4460.
DR   SABIO-RK; Q6Z1Y6; -.
DR   UniPathway; UPA00837; UER00815.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000007752; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030187; P:melatonin biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR045039; NSI-like.
DR   PANTHER; PTHR43626; PTHR43626; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Chloroplast; Cytoplasm; Melatonin biosynthesis; Plastid;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..200
FT                   /note="Serotonin N-acetyltransferase 2, chloroplastic"
FT                   /id="PRO_0000437953"
FT   DOMAIN          55..195
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   200 AA;  21660 MW;  ECC85CE80064EDB4 CRC64;
     MQMQAARPRV GVRPRGGIRP FPLPTLSFNN NSNRSACACA CAVSVSDSEL AARGFAVRRS
     STGLDVGALN EVFARVGFPR RQEERLRRAL EHSEVVWLED SASSSAGRPV AFARAAGDGV
     FNAVVWDVVV EPSCQGLGLG RAVMERLVAD LRGKGVSNIA LYAEPRVVGF YRLLGFAMDP
     DAIRGMAFYR SRQQIQNTSS