I4OMT_GLYEC
ID I4OMT_GLYEC Reviewed; 367 AA.
AC Q84KK6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Isoflavone 4'-O-methyltransferase;
DE Short=GeHI4'OMT;
DE EC=2.1.1.46 {ECO:0000269|PubMed:12610212, ECO:0000269|PubMed:17067644};
DE AltName: Full=2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase;
DE EC=2.1.1.212 {ECO:0000269|PubMed:12610212, ECO:0000269|PubMed:17067644};
DE AltName: Full=S-adenosyl-L-methionine:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase;
GN Name=HI4'OMT;
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, CATALYTIC ACTIVITY, AND INDUCTION BY
RP ELICITOR.
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17067644; DOI=10.1016/j.phytochem.2006.09.010;
RA Akashi T., VanEtten H.D., Sawada Y., Wasmann C.C., Uchiyama H., Ayabe S.;
RT "Catalytic specificity of pea O-methyltransferases suggests gene
RT duplication for (+)-pisatin biosynthesis.";
RL Phytochemistry 67:2525-2530(2006).
CC -!- FUNCTION: 2-hydroxyisoflavanone 4'-O-methyltransferase involved in the
CC biosynthesis of formononetin. Can use 2,7,4'-trihydroxyisoflavanone,
CC (+)-6a-hydroxymaackiain or medicarpin as substrate, but not daidzein or
CC (-)-6a-hydroxymaackiain. {ECO:0000269|PubMed:12610212,
CC ECO:0000269|PubMed:17067644}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4'-hydroxyisoflavone + S-adenosyl-L-methionine = a 4'-
CC methoxyisoflavone + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:31739, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:63328, ChEBI:CHEBI:133959;
CC EC=2.1.1.46; Evidence={ECO:0000269|PubMed:12610212,
CC ECO:0000269|PubMed:17067644};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-2,4',7-trihydroxyisoflavanone + S-adenosyl-L-
CC methionine = (2R,3S)-2,7-dihydroxy-4'-methoxyisoflavanone + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:31371, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:63325,
CC ChEBI:CHEBI:85906; EC=2.1.1.212;
CC Evidence={ECO:0000269|PubMed:12610212, ECO:0000269|PubMed:17067644};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for 2,7,4'-trihydroxyisoflavanone
CC {ECO:0000269|PubMed:17067644};
CC KM=8 uM for (+)-6a-hydroxymaackiain {ECO:0000269|PubMed:17067644};
CC Vmax=20000 pmol/sec/mg enzyme with 2,7,4'-trihydroxyisoflavanone as
CC substrate {ECO:0000269|PubMed:17067644};
CC Vmax=2700 pmol/sec/mg enzyme with (+)-6a-hydroxymaackiain as
CC substrate {ECO:0000269|PubMed:17067644};
CC -!- INDUCTION: Up-regulated by elicitor. {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; AB091684; BAC58011.1; -; mRNA.
DR AlphaFoldDB; Q84KK6; -.
DR SMR; Q84KK6; -.
DR KEGG; ag:BAC58011; -.
DR BRENDA; 2.1.1.212; 2486.
DR SABIO-RK; Q84KK6; -.
DR GO; GO:0102670; F:2,7,4'-trihydroxyisoflavanone-4'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030746; F:isoflavone 4'-O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009701; P:isoflavonoid phytoalexin 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..367
FT /note="Isoflavone 4'-O-methyltransferase"
FT /id="PRO_0000411975"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 209..212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 233..234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 253..254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 367 AA; 40895 MW; 350F21457E9BA30D CRC64;
MAFSTNGSEE IELYHAQIHL YKHVYNFVSS MALKSAMELG IADVIHNHGK PITLPELASA
LKLHPSKVGI LYRFLRLLTH NGFFAKTTVP SQNGKDGEEE EETAYALTPP SKLLVKGKPT
CLASIVRGAL HPSSLDMWRS SEKWFKEDKE LTLFESATGE SFWDFLNKDS ESGTLSMFQE
AMAADSQMFK LALKECRHVF EGLESLVDVG GGTGGVTKLI HEEFPHLKCT VFDQPQVVGN
LSGNENLKFV GGDMFKSIPP ADAVLLKWVL HDWNDELSLK ILKNSKEAIS GKGKEGKVII
IDISIDEASG DRELTELQLD YDLVMLTMFN GKEREKKEWE KLISDAGFSS YKITPICGFK
SLIEVFP
