I4OMT_LOTJA
ID I4OMT_LOTJA Reviewed; 365 AA.
AC Q84KK4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Isoflavone 4'-O-methyltransferase;
DE Short=LjHI4'OMT;
DE EC=2.1.1.46 {ECO:0000269|PubMed:12610212};
DE AltName: Full=2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase;
DE EC=2.1.1.212 {ECO:0000269|PubMed:12610212};
DE AltName: Full=S-adenosyl-L-methionine: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase;
GN Name=HI4'OMT;
OS Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10819328; DOI=10.1093/dnares/7.2.127;
RA Asamizu E., Nakamura Y., Sato S., Tabata S.;
RT "Generation of 7137 non-redundant expressed sequence tags from a legume,
RT Lotus japonicus.";
RL DNA Res. 7:127-130(2000).
RN [2]
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).
CC -!- FUNCTION: 2-hydroxyisoflavanone 4'-O-methyltransferase involved in the
CC biosynthesis of formononetin. Can use 2,7,4'-trihydroxyisoflavanone as
CC substrate, but not daidzein. {ECO:0000269|PubMed:12610212}.
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 -!- 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};
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; AB091686; BAC58013.1; -; mRNA.
DR AlphaFoldDB; Q84KK4; -.
DR SMR; Q84KK4; -.
DR PRIDE; Q84KK4; -.
DR ProMEX; Q84KK4; -.
DR KEGG; ag:BAC58013; -.
DR OMA; CIFEHTH; -.
DR BRENDA; 2.1.1.212; 3076.
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..365
FT /note="Isoflavone 4'-O-methyltransferase"
FT /id="PRO_0000411976"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 207..210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 231..232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 251..252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 365 AA; 40690 MW; D5CA640142142CC2 CRC64;
MDFSSSNGSE DTELSQAQIH LYKHVYNFVS SMALKSAMEL GIADVIHSHG KPITLPELAT
ALNLRPSKIG VLHRFLRLLT HNGFFAKTTV SRGEGAEEET AYGLTPPSKL LVKSNSTCLA
PIVKGALHPS SLDMWRSSKK WFLEDNEELT LFESATGESF WEFLNKETES DTLSMFQEAM
AADSHMFKLA LKECKHVFEG LGSLVDVAGG RGGVTKLIRE AFPHVKCTVF DQPQVVANLT
GDENLNFVGG DMFKSVPPAD AVLLKWVLHD WNDELSLKIL KNCKEAISGR GKEGKVIIID
ISIDETSDDR ELTELKLDYD LVMLTMFNGK EREKKEWEKL IYDAGFSSYK ITPICGFKSL
IEVFP
