M3OM1_PEA
ID M3OM1_PEA Reviewed; 360 AA.
AC O24305;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=(+)-6a-hydroxymaackiain 3-O-methyltransferase 1;
DE EC=2.1.1.270 {ECO:0000269|PubMed:17707445, ECO:0000269|PubMed:1929414};
DE AltName: Full=Isoflavone 4'-O-methyltransferase;
DE EC=2.1.1.46 {ECO:0000269|PubMed:17707445, ECO:0000269|PubMed:1929414};
GN Name=HMM1; Synonyms=HMM6;
OS Pisum sativum (Garden pea).
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; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP COPPER.
RC STRAIN=cv. Alaska;
RX PubMed=9349277; DOI=10.1023/a:1005836508844;
RA Wu Q., Preisig C.L., VanEtten H.D.;
RT "Isolation of the cDNAs encoding (+)6a-hydroxymaackiain 3-O-
RT methyltransferase, the terminal step for the synthesis of the phytoalexin
RT pisatin in Pisum sativum.";
RL Plant Mol. Biol. 35:551-560(1997).
RN [2]
RP FUNCTION, AND INDUCTION BY COPPER.
RX PubMed=1929414; DOI=10.1016/0003-9861(91)90568-4;
RA Preisig C.L., VanEtten H.D., Moreau R.A.;
RT "Induction of 6a-hydroxymaackiain 3-O-methyltransferase and phenylalanine
RT ammonia-lyase mRNA translational activities during the biosynthesis of
RT pisatin.";
RL Arch. Biochem. Biophys. 290:468-473(1991).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 3D-STRUCTURE MODELING.
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).
RN [4]
RP FUNCTION.
RX PubMed=17707445; DOI=10.1016/j.phytochem.2007.06.013;
RA Kaimoyo E., VanEtten H.D.;
RT "Inactivation of pea genes by RNAi supports the involvement of two similar
RT O-methyltransferases in the biosynthesis of (+)-pisatin and of chiral
RT intermediates with a configuration opposite that found in (+)-pisatin.";
RL Phytochemistry 69:76-87(2008).
CC -!- FUNCTION: Methyltransferase involved in the phytoalexin pisatin
CC biosynthesis. Has both 3- and 4'-O-methyltransferase activities. Can
CC use (+)-6a-hydroxymaackiain, 2,7,4'-trihydroxyisoflavanone and with
CC much less activity (+)-medicarpin as substrates, but not (-)-6a-
CC hydroxymaackiain, daidzein, formononetin or isoliquiritigenin. May be
CC involved in formononetin biosynthesis. {ECO:0000269|PubMed:17067644,
CC ECO:0000269|PubMed:17707445, ECO:0000269|PubMed:1929414,
CC ECO:0000269|PubMed:9349277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-6a-hydroxymaackiain + S-adenosyl-L-methionine = (+)-
CC pisatin + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:35471,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43129, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:67347; EC=2.1.1.270;
CC Evidence={ECO:0000269|PubMed:17707445, ECO:0000269|PubMed:1929414};
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:17707445,
CC ECO:0000269|PubMed:1929414};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for 2,7,4'-trihydroxyisoflavanone
CC {ECO:0000269|PubMed:17067644};
CC KM=6 uM for (+)-6a-hydroxymaackiain {ECO:0000269|PubMed:17067644};
CC Vmax=1800 pmol/sec/mg enzyme with 2,7,4'-trihydroxyisoflavanone as
CC substrate {ECO:0000269|PubMed:17067644};
CC Vmax=910 pmol/sec/mg enzyme with (+)-6a-hydroxymaackiain as substrate
CC {ECO:0000269|PubMed:17067644};
CC -!- INDUCTION: Up-regulated by copper. {ECO:0000269|PubMed:1929414,
CC ECO:0000269|PubMed:9349277}.
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; U69554; AAC49856.1; -; mRNA.
DR PIR; T06786; T06786.
DR AlphaFoldDB; O24305; -.
DR SMR; O24305; -.
DR KEGG; ag:AAC49856; -.
DR BRENDA; 2.1.1.270; 4872.
DR SABIO-RK; O24305; -.
DR GO; GO:0102671; F:6a-hydroxymaackiain-3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030746; F:isoflavone 4'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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..360
FT /note="(+)-6a-hydroxymaackiain 3-O-methyltransferase 1"
FT /id="PRO_0000411978"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 202..205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 226..227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 246..247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 360 AA; 40351 MW; 97882D1189A93888 CRC64;
MDFSTNGSEE SELYHAQIHL YKHVYNFVSS MALKSAMELG IADAIHNHGK PMTLPELSSS
LKLHPSKVNI LYRFLRLLTH NGFFAKTTVK SNEGEEETAY VLTPSSKLLV SGKSTCLSSL
VKGALHPSSL DMWGVSKKWF HEDKEQTLFE CATGENYWDF LNKDSDSLSM FQDAMAADSR
LFKLAIQENK HVFEGLESLV DVAGGTGGVA KLIHEAFPHI KCTVFDQPQV VGNLTGNENL
NFVGGDMFKS VPSADAVLLK WVLHDWNDEL SLKILKNSKE AISHKGKDGK VIIIDISIDE
NSDDRGLTEL QLEYDVVMLT MFLGKERTKK EWEKLIYDAG FSRYKITPIC GFKSLIEVYP
