ASMT_ARATH
ID ASMT_ARATH Reviewed; 382 AA.
AC Q9T003;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Acetylserotonin O-methyltransferase {ECO:0000305};
DE EC=2.1.1.4 {ECO:0000269|PubMed:26484897};
DE AltName: Full=N-acetylserotonin O-methyltransferase {ECO:0000303|PubMed:26484897};
DE Short=AtASMT {ECO:0000303|PubMed:26484897};
GN Name=ASMT {ECO:0000303|PubMed:26484897};
GN OrderedLocusNames=At4g35160 {ECO:0000312|Araport:AT4G35160};
GN ORFNames=T12J5.30 {ECO:0000312|EMBL:CAB36723.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND INDUCTION BY CADMIUM.
RX PubMed=26484897; DOI=10.1111/jpi.12289;
RA Byeon Y., Lee H.J., Lee H.Y., Back K.;
RT "Cloning and functional characterization of the Arabidopsis N-
RT acetylserotonin O-methyltransferase responsible for melatonin synthesis.";
RL J. Pineal Res. 60:65-73(2016).
CC -!- FUNCTION: Methyltransferase which catalyzes the transfer of a methyl
CC group onto N-acetylserotonin, producing melatonin (N-acetyl-5-
CC methoxytryptamine). Does not seem to possess caffeate O-
CC methyltransferase activity. {ECO:0000269|PubMed:26484897}.
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:26484897};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=456 uM for N-acetylserotonin {ECO:0000269|PubMed:26484897};
CC KM=1035 uM for serotonin {ECO:0000269|PubMed:26484897};
CC Vmax=6.6 pmol/min/mg enzyme toward N-acetylserotonin
CC {ECO:0000269|PubMed:26484897};
CC Vmax=17.4 pmol/min/mg enzyme toward serotonin
CC {ECO:0000269|PubMed:26484897};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26484897}.
CC -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:26484897}.
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; AL035522; CAB36723.1; -; Genomic_DNA.
DR EMBL; AL161586; CAB80233.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86474.1; -; Genomic_DNA.
DR EMBL; AY099803; AAM20654.1; -; mRNA.
DR EMBL; BT000302; AAN15621.1; -; mRNA.
DR PIR; T04963; T04963.
DR RefSeq; NP_195242.1; NM_119682.4.
DR AlphaFoldDB; Q9T003; -.
DR SMR; Q9T003; -.
DR IntAct; Q9T003; 3.
DR STRING; 3702.AT4G35160.1; -.
DR PaxDb; Q9T003; -.
DR PRIDE; Q9T003; -.
DR ProteomicsDB; 246800; -.
DR EnsemblPlants; AT4G35160.1; AT4G35160.1; AT4G35160.
DR GeneID; 829668; -.
DR Gramene; AT4G35160.1; AT4G35160.1; AT4G35160.
DR KEGG; ath:AT4G35160; -.
DR Araport; AT4G35160; -.
DR TAIR; locus:2132806; AT4G35160.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_7_0_1; -.
DR InParanoid; Q9T003; -.
DR OMA; MMMTANG; -.
DR OrthoDB; 817726at2759; -.
DR PhylomeDB; Q9T003; -.
DR BioCyc; ARA:AT4G35160-MON; -.
DR BRENDA; 2.1.1.4; 399.
DR UniPathway; UPA00837; UER00815.
DR PRO; PR:Q9T003; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T003; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; IDA:TAIR.
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:TAIR.
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..382
FT /note="Acetylserotonin O-methyltransferase"
FT /id="PRO_0000442916"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 308
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 347
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
SQ SEQUENCE 382 AA; 42614 MW; F2C5FD8C558C3A9B CRC64;
MSSDQLSKFL DRNKMEDNKR KVLDEEAKAS LDIWKYVFGF ADIAAAKCAI DLKIPEAIEN
HPSSQPVTLA ELSSAVSASP SHLRRIMRFL VHQGIFKEIP TKDGLATGYV NTPLSRRLMI
TRRDGKSLAP FVLFETTPEM LAPWLRLSSV VSSPVNGSTP PPFDAVHGKD VWSFAQDNPF
LSDMINEAMA CDARRVVPRV AGACHGLFDG VTTMVDVGGG TGETMGMLVK EFPWIKGFNF
DLPHVIEVAE VLDGVENVEG DMFDSIPACD AIFIKWVLHD WGDKDCIKIL KNCKEAVPPN
IGKVLIVESV IGENKKTMIV DERDEKLEHV RLMLDMVMMA HTSTGKERTL KEWDFVLKEA
GFARYEVRDI DDVQSLIIAY RS
