FAOMT_VITVI
ID FAOMT_VITVI Reviewed; 235 AA.
AC C7AE94;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Flavonoid 3',5'-methyltransferase;
DE EC=2.1.1.267 {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
DE AltName: Full=Anthocyanin-O-methyltransferase;
DE Short=VvAOMT;
GN Name=FAOMT;
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, PATHWAY, COFACTOR, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Syrah;
RX PubMed=19525322; DOI=10.1104/pp.109.140376;
RA Hugueney P., Provenzano S., Verries C., Ferrandino A., Meudec E.,
RA Batelli G., Merdinoglu D., Cheynier V., Schubert A., Ageorges A.;
RT "A novel cation-dependent o-methyltransferase involved in anthocyanin
RT methylation in grapevine.";
RL Plant Physiol. 150:2057-2070(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND PATHWAY.
RC STRAIN=cv. Cabernet Sauvignon;
RX PubMed=20580386; DOI=10.1016/j.phytochem.2010.05.027;
RA Lucker J., Martens S., Lund S.T.;
RT "Characterization of a Vitis vinifera cv. Cabernet Sauvignon 3',5'-O-
RT methyltransferase showing strong preference for anthocyanins and
RT glycosylated flavonols.";
RL Phytochemistry 71:1474-1484(2010).
CC -!- FUNCTION: Mediates O-methylation of anthocyanins. Anthocyanins are
CC major pigments in grapes: at ripening initiation in red grapevine
CC berries, the exocarp turns color from green to red and then to purple
CC due to the accumulation and extent of methylation of anthocyanins.
CC Catalyzes both 3' and 5' O-methylation of anthocyanins, with a
CC preference for glycosylated substrates. Active on both anthocyanins and
CC flavonols in vitro. Most active with delphinidin 3-glucoside but also
CC acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and
CC quercetin 3-glucoside. Not able to methylate flavan type skeletons with
CC chiral centers, such as catechins or dihydroquercetin.
CC {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + a 3'-hydroxyflavonoid = S-adenosyl-
CC L-homocysteine + a 3'-methoxyflavonoid.; EC=2.1.1.267;
CC Evidence={ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + a 5'-hydroxy-3'-methoxyflavonoid =
CC S-adenosyl-L-homocysteine + a 3',5'-dimethoxyflavonoid.;
CC EC=2.1.1.267;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=43 uM for cyanidin 3-glucoside {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC KM=7.6 uM for cyanidin 3-glucoside {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC KM=44 uM for delphinidin 3-glucoside {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC KM=24 uM for quercetin 3-glucoside {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC KM=2.7 uM for quercetin 3-glucoside {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC KM=74 uM for cyanidin {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC KM=33 uM for quercetin {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC KM=19 uM for myricetin {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC Note=kcat is 0.090 sec(-1) with cyanidin 3-glucoside
CC (PubMed:19525322). kcat is 2.3825 sec(-1) with cyanidin 3-glucoside
CC (PubMed:20580386). kcat is 0.118 sec(-1) with delphinidin 3-glucoside
CC (PubMed:19525322). kcat is 0.1 sec(-1) with quercetin 3-glucoside
CC (PubMed:19525322). kcat is 0.8976 sec(-1) with quercetin 3-glucoside
CC (PubMed:20580386). kcat is 0.084 sec(-1) with cyanidin
CC (PubMed:19525322). kcat is 0.112 sec(-1) with quercetin
CC (PubMed:19525322). kcat is 0.128sec(-1) with myricetin
CC (PubMed:19525322). {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC pH dependence:
CC Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:19525322,
CC ECO:0000269|PubMed:20580386};
CC Temperature dependence:
CC Optimum temperature is 49 degrees Celsius.
CC {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC {ECO:0000269|PubMed:19525322, ECO:0000269|PubMed:20580386}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19525322}.
CC -!- DEVELOPMENTAL STAGE: Expressed in berries at start ripening (veraison),
CC when the concentrations of methylated anthocyanins begin to increase.
CC {ECO:0000269|PubMed:19525322}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; FJ460168; ACO52469.1; -; mRNA.
DR EMBL; HM142924; ADJ57332.1; -; mRNA.
DR AlphaFoldDB; C7AE94; -.
DR SMR; C7AE94; -.
DR STRING; 29760.VIT_01s0010g03510.t01; -.
DR EnsemblPlants; Vitvi01g04438_t001; Vitvi01g04438_P001; Vitvi01g04438.
DR Gramene; Vitvi01g04438_t001; Vitvi01g04438_P001; Vitvi01g04438.
DR eggNOG; KOG1663; Eukaryota.
DR BRENDA; 2.1.1.267; 6671.
DR SABIO-RK; C7AE94; -.
DR UniPathway; UPA00009; -.
DR ExpressionAtlas; C7AE94; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070448; F:laricitrin 5'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0033799; F:myricetin 3'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033485; P:cyanidin 3-O-glucoside biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033486; P:delphinidin 3-O-glucoside biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0043473; P:pigmentation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..235
FT /note="Flavonoid 3',5'-methyltransferase"
FT /id="PRO_0000422557"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 75..76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 178
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ SEQUENCE 235 AA; 26397 MW; 45D567C1D90915C5 CRC64;
MSSSSHRGIL KTEALTKYLL ETSAYPREHE QLKGLREATV EKHKYWSLMN VPVDEGLFIS
MLLKIMNAKK TIELGVFTGY SLLATALALP QDGKIIAVDP DKEAYQTGVP FIKKAGVEHK
INFIQSDAMS VLNDLIADGK EEGTLDFAMV DADKENYLNY HELLLKLVRV GGIIAYDNTL
WFGSVARSEE EEMMDFERAG RVHLMKLNKF LASDPRVELS HLSIGDGVAL CRRLY
