ASMT3_ORYSJ
ID ASMT3_ORYSJ Reviewed; 366 AA.
AC Q8VWG4; A0A0P0XRW1; Q7XH65;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Acetylserotonin O-methyltransferase 3 {ECO:0000305};
DE Short=OsASMT3 {ECO:0000303|PubMed:24134674};
DE EC=2.1.1.4 {ECO:0000269|PubMed:24033370};
GN Name=ASMT3 {ECO:0000303|PubMed:24033370};
GN OrderedLocusNames=Os10g0118000 {ECO:0000312|EMBL:BAT09680.1},
GN LOC_Os10g02840 {ECO:0000312|EMBL:AAP51889.2};
GN ORFNames=OSJNBa0023I19.18 {ECO:0000312|EMBL:AAL34945.1},
GN OSJNBa0079B05.1 {ECO:0000312|EMBL:AAL31646.1};
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 MRNA] (ISOFORM 2).
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, AND TISSUE SPECIFICITY.
RX PubMed=24033370; DOI=10.1111/jpi.12088;
RA Park S., Byeon Y., Back K.;
RT "Functional analyses of three ASMT gene family members in rice plants.";
RL J. Pineal Res. 55:409-415(2013).
RN [7]
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).
CC -!- FUNCTION: Methyltransferase which catalyzes the transfer of a methyl
CC group onto N-acetylserotonin, producing melatonin (N-acetyl-5-
CC methoxytryptamine). {ECO:0000269|PubMed:24033370}.
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:0000269|PubMed:24033370};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24134674}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VWG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VWG4-2; Sequence=VSP_058578;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, shoots, leaves,
CC stems and flowers. {ECO:0000269|PubMed:24033370}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAT09680.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079037; AAL34945.1; -; Genomic_DNA.
DR EMBL; AC079179; AAL31646.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP51889.2; -; Genomic_DNA.
DR EMBL; AP008216; BAF25972.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT09680.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK069721; BAG91569.1; -; mRNA.
DR RefSeq; XP_015613323.1; XM_015757837.1. [Q8VWG4-1]
DR AlphaFoldDB; Q8VWG4; -.
DR SMR; Q8VWG4; -.
DR STRING; 4530.OS10T0118000-01; -.
DR PRIDE; Q8VWG4; -.
DR GeneID; 4347993; -.
DR KEGG; osa:4347993; -.
DR InParanoid; Q8VWG4; -.
DR OrthoDB; 817726at2759; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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:0030187; P:melatonin biosynthetic process; IDA: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; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
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; PF08100; Dimerisation; 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 Alternative splicing; Cytoplasm; Melatonin biosynthesis; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..366
FT /note="Acetylserotonin O-methyltransferase 3"
FT /id="PRO_0000437949"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 302
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 332
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 232
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:0000250|UniProtKB:P28002"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT VAR_SEQ 1..185
FT /note="MAQRVQEEDEQMTSTDDLIQAEIELYHHCFAFIKSTALRAATDLCISDAIHR
FT NGGAATLSDLALNIGLHPTKLSHLRRLMRVPTVSGVFAVEDHNGEAMYTLTRVSRLLLN
FT GDGERTHALSHLVRVLVNPLTVASHFSIHEWFTIEQAAAMTPFEVAHGCTRWEIIANDA
FT KDGSVFNTAMVEDSR -> MTPFEVAHGCTRWEIIANDAKDGSVFNTAMVEDSR (in
FT isoform 2)"
FT /id="VSP_058578"
SQ SEQUENCE 366 AA; 40303 MW; CB134D83432A8151 CRC64;
MAQRVQEEDE QMTSTDDLIQ AEIELYHHCF AFIKSTALRA ATDLCISDAI HRNGGAATLS
DLALNIGLHP TKLSHLRRLM RVPTVSGVFA VEDHNGEAMY TLTRVSRLLL NGDGERTHAL
SHLVRVLVNP LTVASHFSIH EWFTIEQAAA MTPFEVAHGC TRWEIIANDA KDGSVFNTAM
VEDSRVAMDI ILKESCGVFQ GISSLVDVGG GHGAAAAAIA TAFPNIKCTV LDLPHIVAEA
PTTHSNIQFV GGDFFEFIPA ADVVLLKYIL HAWQDDDCVK ILRRCKEAIL ARDAGGKVII
IEVVVGIGPK EIVPKEMQIL FDVFMMYVDG IEREEHEWKK IFLEAGFSDY KITPVLGARS
IIEVYP
