SOMT2_SOYBN
ID SOMT2_SOYBN Reviewed; 358 AA.
AC C6TAY1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Flavonoid 4'-O-methyltransferase;
DE EC=2.1.1.231;
DE AltName: Full=S-adenosyl-L-methionine-dependent methyltransferase 2;
DE Short=SOMT-2;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Paldal;
RX PubMed=15961179; DOI=10.1016/j.jbiotec.2005.04.004;
RA Kim D.H., Kim B.G., Lee Y., Ryu J.Y., Lim Y., Hur H.G., Ahn J.H.;
RT "Regiospecific methylation of naringenin to ponciretin by soybean O-
RT methyltransferase expressed in Escherichia coli.";
RL J. Biotechnol. 119:155-162(2005).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes the 4'-methylation of naringenin (4',5,7-trihydroxyflavanone)
CC into ponciretin (4'-methoxy-5,7-dihydroxyflavanone). In vitro, also
CC able to convert apigenin, daidzein, genistein and quercetin into the
CC 4'-O-methylated compounds acacetin, formononetin, biochanine A and 4'-
CC methylated quercetin, respectively. {ECO:0000269|PubMed:15961179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4'-hydroxyflavanone + S-adenosyl-L-methionine = a 4'-
CC methoxyflavanone + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:31743, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:140331, ChEBI:CHEBI:140332;
CC EC=2.1.1.231; Evidence={ECO:0000269|PubMed:15961179};
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; BT094674; ACU18983.1; -; mRNA.
DR AlphaFoldDB; C6TAY1; -.
DR SMR; C6TAY1; -.
DR STRING; 3847.GLYMA08G27070.1; -.
DR PRIDE; C6TAY1; -.
DR eggNOG; KOG3178; Eukaryota.
DR BRENDA; 2.1.1.231; 2483.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0102767; F:flavanone 4'-O-methyltransferase activity; IEA:UniProtKB-EC.
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: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..358
FT /note="Flavonoid 4'-O-methyltransferase"
FT /id="PRO_0000418737"
FT REGION 155..173
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 122..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 358 AA; 40436 MW; B8C7D1C0DD5B709E CRC64;
MASPLNNGRK ASEIFQGQAL LYKHLLGFID SKCLKWMVEL DIPDIIHSHS HGQPITFSEL
VSILQVPPTK TRQVQSLMRY LAHNGFFEIV RIHDNIEAYA LTAASELLVK SSELSLAPMV
EYFLEPNCQG AWNQLKRWVH EEDLTVFGVS LGTPFWDFIN KDPAYNKSFN EAMACDSQML
NLAFRDCNWV FEGLESIVDV GGGTGITAKI ICEAFPKLKC MVLERPNVVE NLSGSNNLTF
VGGDMFKCIP KADAVLLKLV LHNWNDNDCM KILENCKEAI SGESKTGKVV VIDTVINENK
DERQVTELKL LMDVHMACII NGKERKEEDW KKLFMEAGFQ SYKISPFTGY LSLIEIYP
