ID   D7OMT_GLYEC             Reviewed;         357 AA.
AC   Q84KK5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Isoflavone 7-O-methyltransferase;
DE            EC=2.1.1.150;
DE   AltName: Full=Daidzein 7-O-methyltransferase;
GN   Name=D7OMT;
OS   Glycyrrhiza echinata (Licorice).
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; Hologalegina; IRL clade; Galegeae; Glycyrrhiza.
OX   NCBI_TaxID=46348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12610212; DOI=10.1093/pcp/pcg034;
RA   Akashi T., Sawada Y., Shimada N., Sakurai N., Aoki T., Ayabe S.;
RT   "cDNA cloning and biochemical characterization of S-adenosyl-L-methionine:
RT   2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase, a critical enzyme of
RT   the legume isoflavonoid phytoalexin pathway.";
RL   Plant Cell Physiol. 44:103-112(2003).
CC   -!- FUNCTION: 7-O-methyltransferase involved in the biosynthesis of
CC       isoformononetin. Can use daidzein as substrate, but not medicarpin or
CC       2,7,4'-trihydroxyisoflavanone. {ECO:0000269|PubMed:12610212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 7-hydroxyisoflavone + S-adenosyl-L-methionine = a 7-
CC         methoxyisoflavone + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:17933, ChEBI:CHEBI:15378, ChEBI:CHEBI:55465,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:140356;
CC         EC=2.1.1.150; Evidence={ECO:0000269|PubMed:12610212};
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; AB091685; BAC58012.1; -; mRNA.
DR   AlphaFoldDB; Q84KK5; -.
DR   SMR; Q84KK5; -.
DR   GO; GO:0033800; F:isoflavone 7-O-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009717; P:isoflavonoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..357
FT                   /note="Isoflavone 7-O-methyltransferase"
FT                   /id="PRO_0000411980"
FT   ACT_SITE        262
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         200..203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         224..225
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         244..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   357 AA;  40274 MW;  6E4F1AA94E5EAB9E CRC64;
     MASSINGRKP SEIFQGQALL YRHIYAFIDS MCLKWIVELD IPNIIHNHGK PITVSELVSI
     LKVPQTKAGN VQRIMRYMAH NGFFERVRIQ EEQEENEAYA LTAASELLVK GSELCLAPMV
     ECVLDPTLSG SYHQLKKWIY EEDLTLFGVS LGSHFWEFLN ENPEYNKSFN DAMASDSQMI
     NLALRDCNSG FEGVESIVDV GGGIGTTAKI ICDTFPNLKC IVFDRPKVVE NLSGTNNLSY
     VGGDMFQSVP KADAVLLKWI LHNWTDNDCR RILEKCKEAV SSDGEKGKVI IIEMVINENQ
     DEHEITGTKL LMDVNMACLN GKERSEEEWK KLFIEAGFRD YKISPLTGFL SLIEVYP