ASMT1_ORYSJ
ID ASMT1_ORYSJ Reviewed; 364 AA.
AC Q6EPG8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Acetylserotonin O-methyltransferase 1 {ECO:0000305};
DE Short=OsASMT1 {ECO:0000303|PubMed:24134674};
DE EC=2.1.1.4 {ECO:0000269|PubMed:21210840};
GN Name=ASMT1 {ECO:0000303|PubMed:24033370};
GN Synonyms=ASMT {ECO:0000303|PubMed:21210840};
GN OrderedLocusNames=Os09g0344500 {ECO:0000312|EMBL:BAT07597.1},
GN LOC_Os09g17560 {ECO:0000305};
GN ORFNames=OSJNBb0057I13.39 {ECO:0000312|EMBL:BAD29452.1},
GN OSJNBb0085I16.5 {ECO:0000312|EMBL:BAD29092.1};
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 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 [5]
RP INDUCTION BY COPPER.
RX PubMed=18676621; DOI=10.1093/jxb/ern196;
RA Sudo E., Itouga M., Yoshida-Hatanaka K., Ono Y., Sakakibara H.;
RT "Gene expression and sensitivity in response to copper stress in rice
RT leaves.";
RL J. Exp. Bot. 59:3465-3474(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=21210840; DOI=10.1111/j.1600-079x.2010.00841.x;
RA Kang K., Kong K., Park S., Natsagdorj U., Kim Y.S., Back K.;
RT "Molecular cloning of a plant N-acetylserotonin methyltransferase and its
RT expression characteristics in rice.";
RL J. Pineal Res. 50:304-309(2011).
RN [7]
RP INDUCTION BY BUTAFENACIL.
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, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY DARK.
RX PubMed=22747959; DOI=10.1111/j.1600-079x.2012.01019.x;
RA Park S., Byeon Y., Kim Y.S., Back K.;
RT "Kinetic analysis of purified recombinant rice N-acetylserotonin
RT methyltransferase and peak melatonin production in etiolated rice shoots.";
RL J. Pineal Res. 54:139-144(2013).
RN [9]
RP FUNCTION, 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 [10]
RP INDUCTION BY UV-C.
RX PubMed=24035516; DOI=10.1016/j.phytochem.2013.08.012;
RA Park H.L., Lee S.W., Jung K.H., Hahn T.R., Cho M.H.;
RT "Transcriptomic analysis of UV-treated rice leaves reveals UV-induced
RT phytoalexin biosynthetic pathways and their regulatory networks in rice.";
RL Phytochemistry 96:57-71(2013).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND 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:21210840,
CC ECO:0000269|PubMed:22747959, ECO:0000269|PubMed:24033370,
CC ECO:0000269|PubMed:24134674}.
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:21210840};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=222 uM for N-acetylserotonin (at 55 degrees Celsius)
CC {ECO:0000269|PubMed:24134674};
CC KM=864 uM for N-acetylserotonin (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:22747959};
CC Vmax=9 nmol/min/mg enzyme with N-acetylserotonin as substrate at 55
CC degrees Celsius) {ECO:0000269|PubMed:24134674};
CC Vmax=13.8 pmol/min/mg enzyme with N-acetylserotonin as substrate (at
CC 30 degrees Celsius) {ECO:0000269|PubMed:24134674};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:24134674};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24134674}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:24033370}.
CC -!- INDUCTION: By senescence, abscisic acid (ABA), acifluorfen, salt and
CC cadmium (PubMed:21210840). Induced by copper (PubMed:18676621,
CC PubMed:21210840). Induced by butafenacil (PubMed:22998587). Induced in
CC dark-grown etiolated shoot (PubMed:22747959). Induced by UV-C
CC (PubMed:24035516). {ECO:0000269|PubMed:18676621,
CC ECO:0000269|PubMed:21210840, ECO:0000269|PubMed:22747959,
CC ECO:0000269|PubMed:22998587, ECO:0000269|PubMed:24035516}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AP005700; BAD29092.1; -; Genomic_DNA.
DR EMBL; AP005881; BAD29452.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24845.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT07597.1; -; Genomic_DNA.
DR EMBL; AK072740; BAG93122.1; -; mRNA.
DR RefSeq; XP_015610997.1; XM_015755511.1.
DR RefSeq; XP_015610998.1; XM_015755512.1.
DR AlphaFoldDB; Q6EPG8; -.
DR SMR; Q6EPG8; -.
DR STRING; 4530.OS09T0344500-01; -.
DR PaxDb; Q6EPG8; -.
DR PRIDE; Q6EPG8; -.
DR EnsemblPlants; Os09t0344500-01; Os09t0344500-01; Os09g0344500.
DR GeneID; 4346795; -.
DR Gramene; Os09t0344500-01; Os09t0344500-01; Os09g0344500.
DR KEGG; osa:4346795; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_7_0_1; -.
DR InParanoid; Q6EPG8; -.
DR OMA; NEQVMST; -.
DR OrthoDB; 817726at2759; -.
DR SABIO-RK; Q6EPG8; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
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 Cytoplasm; Melatonin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..364
FT /note="Acetylserotonin O-methyltransferase 1"
FT /id="PRO_0000437947"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 300
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 330
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
SQ SEQUENCE 364 AA; 40095 MW; B77C00F1EC496AB1 CRC64;
MAQNVQENEQ VMSTEDLLQA QIELYHHCLA FIKSMALRAA TDLRIPDAIH CNGGAATLTD
LAAHVGLHPT KLSHLRRLMR VLTLSGIFTV HDGDGEATYT LTRVSRLLLS DGVERTHGLS
QMVRVFVNPV AVASQFSLHE WFTVEKAAAV SLFEVAHGCT RWEMIANDSK DGSMFNAGMV
EDSSVAMDII LRKSSNVFRG INSLVDVGGG YGAVAAAVVR AFPDIKCTVL DLPHIVAKAP
SNNNIQFVGG DLFEFIPAAD VVLLKCILHC WQHDDCVKIM RRCKEAISAR DAGGKVILIE
VVVGIGSNET VPKEMQLLFD VFMMYTDGIE REEHEWKKIF LEAGFSDYKI IPVLGVRSII
EVYP
