ROMT_VITVI
ID ROMT_VITVI Reviewed; 357 AA.
AC B6VJS4; F6H518;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Trans-resveratrol di-O-methyltransferase;
DE EC=2.1.1.240;
DE AltName: Full=Resveratrol O-methyltransferase;
DE Short=ROMT;
DE Short=VvROMT;
GN Name=ROMT; OrderedLocusNames=VIT_12s0028g01880;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=cv. Cabernet Sauvignon; TISSUE=Leaf;
RX PubMed=18799660; DOI=10.1104/pp.108.126003;
RA Schmidlin L., Poutaraud A., Claudel P., Mestre P., Prado E.,
RA Santos-Rosa M., Wiedemann-Merdinoglu S., Karst F., Merdinoglu D.,
RA Hugueney P.;
RT "A stress-inducible resveratrol O-methyltransferase involved in the
RT biosynthesis of pterostilbene in grapevine.";
RL Plant Physiol. 148:1630-1639(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- FUNCTION: Catalyzes the biosynthesis of pterostilbene from resveratrol.
CC Pterostilbene has both antifungal and pharmacological properties. Also
CC has activity toward resveratrol monomethyl ether (RME).
CC {ECO:0000269|PubMed:18799660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 S-adenosyl-L-methionine + trans-resveratrol = 2 H(+) +
CC pterostilbene + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32103,
CC ChEBI:CHEBI:8630, ChEBI:CHEBI:15378, ChEBI:CHEBI:45713,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.240;
CC Evidence={ECO:0000269|PubMed:18799660};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for resveratrol {ECO:0000269|PubMed:18799660};
CC KM=14 uM for resveratrol monomethyl ether
CC {ECO:0000269|PubMed:18799660};
CC -!- INDUCTION: Expression in leaves is induced by different stresses, such
CC as downy mildew (P.viticola) infection, ultraviolet light, and AlCl(3)
CC treatment. {ECO:0000269|PubMed:18799660}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; FM178870; CAQ76879.1; -; mRNA.
DR EMBL; FN595235; CCB47386.1; -; Genomic_DNA.
DR EMBL; FN597034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; B6VJS4; -.
DR SMR; B6VJS4; -.
DR STRING; 29760.VIT_12s0028g01880.t01; -.
DR EnsemblPlants; Vitvi12g02241_t001; Vitvi12g02241_P001; Vitvi12g02241.
DR Gramene; Vitvi12g02241_t001; Vitvi12g02241_P001; Vitvi12g02241.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_7_0_1; -.
DR InParanoid; B6VJS4; -.
DR BioCyc; MetaCyc:MON-16020; -.
DR BRENDA; 2.1.1.240; 6671.
DR Proteomes; UP000009183; Chromosome 12.
DR ExpressionAtlas; B6VJS4; baseline and differential.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0102303; F:resveratrol 3,5-O-dimethyltransferase activity; IEA:UniProtKB-EC.
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: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 Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..357
FT /note="Trans-resveratrol di-O-methyltransferase"
FT /id="PRO_0000418736"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT CONFLICT 149
FT /note="Y -> H (in Ref. 1; CAQ76879)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="S -> P (in Ref. 1; CAQ76879)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="N -> D (in Ref. 1; CAQ76879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40100 MW; D306FC2AC0F48599 CRC64;
MDLANGVISA ELLHAQAHVW NHIFNFIKSM SLKCAIQLGI PDIIHNHGKP MTLPELVAKL
PVHPKRSQCV YRLMRILVHS GFLAAQRVQQ GKEEEGYVLT DASRLLLMDD SLSIRPLVLA
MLDPILTKPW HYLSAWFQND DPTPFHTAYE RSFWDYAGHE PQLNNSFNEA MASDARLLTS
VLLKEGQGVF AGLNSLVDVG GGTGKVAKAI ANAFPHLNCT VLDLSHVVAG LQGSKNLNYF
AGDMFEAIPP ADAILLKWIL HDWSNEECVK ILKRCREAIP SKENGGKVII IDMIMMKNQG
DYKSTETQLF FDMTMMIFAP GRERDENEWE KLFLDAGFSH YKITPILGLR SLIEVYP
