SNAT1_ORYSJ
ID SNAT1_ORYSJ Reviewed; 254 AA.
AC Q5KQI6; A3B560; B7E3M6; Q0DHA1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Serotonin N-acetyltransferase 1, chloroplastic {ECO:0000303|PubMed:27121038};
DE Short=OsSNAT1 {ECO:0000303|PubMed:27121038};
DE EC=2.3.1.87 {ECO:0000269|PubMed:22998587, ECO:0000269|PubMed:24134674, ECO:0000269|PubMed:27121038};
DE AltName: Full=Acetyltransferase NSI homolog {ECO:0000305};
DE AltName: Full=Nuclear shuttle protein-interacting protein homolog {ECO:0000305};
DE Flags: Precursor;
GN Name=SNAT1 {ECO:0000303|PubMed:27121038};
GN Synonyms=GNAT5 {ECO:0000303|PubMed:22998587}, NSI {ECO:0000305},
GN SNAT {ECO:0000303|PubMed:22998587};
GN OrderedLocusNames=Os05g0481000, LOC_Os05g40260;
GN ORFNames=OsJ_018182, OsJ_18949 {ECO:0000312|EMBL:EEE64117.1},
GN OSJNBa0095J22.4;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=22998587; DOI=10.1111/jpi.12011;
RA Kang K., Lee K., Park S., Byeon Y., Back K.;
RT "Molecular cloning of rice serotonin N-acetyltransferase, the penultimate
RT gene in plant melatonin biosynthesis.";
RL J. Pineal Res. 55:7-13(2013).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24134674; DOI=10.1111/jpi.12103;
RA Byeon Y., Lee H.Y., Lee K., Park S., Back K.;
RT "Cellular localization and kinetics of the rice melatonin biosynthetic
RT enzymes SNAT and ASMT.";
RL J. Pineal Res. 56:107-114(2014).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
RN [10]
RP FUNCTION.
RX PubMed=28118490; DOI=10.1111/jpi.12392;
RA Lee K., Back K.;
RT "Overexpression of rice serotonin N-acetyltransferase 1 in transgenic rice
RT plants confers resistance to cadmium and senescence and increases grain
RT yield.";
RL J. Pineal Res. 62:0-0(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 92-254.
RX PubMed=32595985; DOI=10.1016/j.jare.2020.06.004;
RA Zhou Y., Liao L., Liu X., Liu B., Chen X., Guo Y., Huang C., Zhao Y.,
RA Zeng Z.;
RT "Crystal structure of Oryza sativa TDC reveals the substrate specificity
RT for TDC-mediated melatonin biosynthesis.";
RL J. Adv. Res. 24:501-511(2020).
CC -!- FUNCTION: Catalyzes the N-acetylation of serotonin into N-
CC acetylserotonin, the penultimate step in the synthesis of melatonin
CC (PubMed:22998587, PubMed:24134674, PubMed:27121038, PubMed:28118490).
CC Catalyzes in vitro the N-acetylation of tryptamine to produce N-
CC acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine
CC to produce N-acetyltyramine (PubMed:27121038).
CC {ECO:0000269|PubMed:22998587, ECO:0000269|PubMed:24134674,
CC ECO:0000269|PubMed:27121038, ECO:0000269|PubMed:28118490}.
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:22998587,
CC ECO:0000269|PubMed:24134674, ECO:0000269|PubMed:27121038};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25218;
CC Evidence={ECO:0000269|PubMed:22998587, ECO:0000269|PubMed:24134674,
CC 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=270 uM for serotonin (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:24134674};
CC KM=385 uM for serotonin (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22998587};
CC KM=836 uM for tryptamine (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22998587};
CC KM=375 uM for 5-methoxytryptamine (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22998587};
CC Vmax=3.3 nmol/min/mg enzyme with serotonin as substrate (at 55
CC degrees Celsius) {ECO:0000269|PubMed:24134674};
CC Vmax=282 pmol/min/mg enzyme with serotonin as substrate (at 30
CC degrees Celsius) {ECO:0000269|PubMed:22998587};
CC Vmax=480 pmol/min/mg enzyme with tryptamine as substrate (at 30
CC degrees Celsius) {ECO:0000269|PubMed:22998587};
CC Vmax=390 pmol/min/mg enzyme with 5-methoxytryptamine as substrate (at
CC 30 degrees Celsius) {ECO:0000269|PubMed:22998587};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:22998587};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:24134674};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:24134674}. Nucleus {ECO:0000250|UniProtKB:Q7X9V3}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:22998587}.
CC -!- INDUCTION: Down-regulated by cadmium. {ECO:0000269|PubMed:27121038}.
CC -!- MISCELLANEOUS: Plants overexpressing SNAT1 exhibit tolerance to
CC cadmium, delayed leaf senescence, and increased grain yield due to
CC increased panicle number. {ECO:0000269|PubMed:28118490}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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; AC137619; AAW56866.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17772.2; -; Genomic_DNA.
DR EMBL; AP014961; BAS94577.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64117.1; -; Genomic_DNA.
DR EMBL; AK059369; BAG86973.1; -; mRNA.
DR RefSeq; XP_015637887.1; XM_015782401.1.
DR PDB; 6K5M; X-ray; 1.79 A; A=92-254.
DR PDB; 7DAI; X-ray; 2.30 A; A/B/C=91-254.
DR PDB; 7DAJ; X-ray; 2.30 A; A/B=91-254.
DR PDB; 7DAK; X-ray; 2.80 A; A/B=91-254.
DR PDB; 7DAL; X-ray; 2.50 A; A/B=91-254.
DR PDBsum; 6K5M; -.
DR PDBsum; 7DAI; -.
DR PDBsum; 7DAJ; -.
DR PDBsum; 7DAK; -.
DR PDBsum; 7DAL; -.
DR AlphaFoldDB; Q5KQI6; -.
DR SMR; Q5KQI6; -.
DR STRING; 4530.OS05T0481000-01; -.
DR PaxDb; Q5KQI6; -.
DR PRIDE; Q5KQI6; -.
DR EnsemblPlants; Os05t0481000-01; Os05t0481000-01; Os05g0481000.
DR GeneID; 4339123; -.
DR Gramene; Os05t0481000-01; Os05t0481000-01; Os05g0481000.
DR KEGG; osa:4339123; -.
DR eggNOG; ENOG502QSCQ; Eukaryota.
DR HOGENOM; CLU_086503_0_0_1; -.
DR InParanoid; Q5KQI6; -.
DR OMA; VPFHANY; -.
DR OrthoDB; 1429454at2759; -.
DR BRENDA; 2.3.1.87; 8948.
DR SABIO-RK; Q5KQI6; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q5KQI6; baseline and differential.
DR Genevisible; Q5KQI6; OS.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IEA:EnsemblPlants.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0030187; P:melatonin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0062055; P:photosynthetic state transition; IEA:EnsemblPlants.
DR GO; GO:0046739; P:transport of virus in multicellular host; IEA:EnsemblPlants.
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 3D-structure; Acyltransferase; Chloroplast; Melatonin biosynthesis;
KW Nucleus; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..74
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 75..254
FT /note="Serotonin N-acetyltransferase 1, chloroplastic"
FT /id="PRO_0000333288"
FT DOMAIN 111..254
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6K5M"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:6K5M"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:6K5M"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:6K5M"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:6K5M"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:6K5M"
FT STRAND 181..192
FT /evidence="ECO:0007829|PDB:6K5M"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6K5M"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:7DAL"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:6K5M"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6K5M"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6K5M"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:6K5M"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:7DAJ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:6K5M"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:7DAJ"
SQ SEQUENCE 254 AA; 27660 MW; A3AFED2D6EC0D51D CRC64;
MAPAASASAS AVVTPSSFRC VPTASCGLGA RGKAPAPRRL LHDHAQGKKR AAATWSLKAG
LWDSLRSGFL KSNNSTETVE PPSAPIEEEE PLPEELVLLE RTLADGSTEQ IIFSSAGDVN
VYDLQALCDK VGWPRRPLTK IAASLRNSYL VATLHSVTMP SKAEGEERKQ LIGMARATSD
HAFNATIWDV LVDPSYQGQG LGKALMEKVI RTLLQRDISN ITLFADNKVV DFYKNLGFEA
DPQGIKGMFW YPRF
