M3OM2_PEA
ID M3OM2_PEA Reviewed; 360 AA.
AC P0DH60;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=(+)-6a-hydroxymaackiain 3-O-methyltransferase 2;
DE EC=2.1.1.270 {ECO:0000269|PubMed:17067644, ECO:0000269|PubMed:9349277};
GN Name=HMM2;
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, 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 [3]
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: 3-O-methyltransferase involved in the phytoalexin pisatin
CC biosynthesis. Can use (+)-6a-hydroxymaackiain, (+)-maackiain and with a
CC lower activity (+)-medicarpin and 2,7,4'-trihydroxyisoflavanone as
CC substrates, but not (-)-6a-hydroxymaackiain, daidzein, formononetin or
CC isoliquiritigenin. {ECO:0000269|PubMed:17067644,
CC ECO:0000269|PubMed:17707445, 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:17067644, ECO:0000269|PubMed:9349277};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for 2,7,4'-trihydroxyisoflavanone
CC {ECO:0000269|PubMed:17067644};
CC KM=0.5 uM for (+)-6a-hydroxymaackiain {ECO:0000269|PubMed:17067644};
CC Vmax=340 pmol/sec/mg enzyme with 2,7,4'-trihydroxyisoflavanone as
CC substrate {ECO:0000269|PubMed:17067644};
CC Vmax=520 pmol/sec/mg enzyme with (+)-6a-hydroxymaackiain as substrate
CC {ECO:0000269|PubMed:17067644};
CC -!- INDUCTION: Up-regulated by copper. {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 AlphaFoldDB; P0DH60; -.
DR SMR; P0DH60; -.
DR SABIO-RK; P0DH60; -.
DR GO; GO:0102671; F:6a-hydroxymaackiain-3-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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
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 2"
FT /id="PRO_0000411979"
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; 40380 MW; 35C321AA3652130B CRC64;
MDFSTNGSEE SELYHAQIHL YKHIYNFVSS MALKSAVELG IADAIHNHGK PMTLPELASS
LKLHPSKVNI LYRFLRLLTH NGFFAKTTVK SNGEEEETAY VLTPSSKLLV SGKSTCLSSV
VKGALHPISL DLWGVSKKWF HEDKEQTLFE CATGENYWDF LNKDSDYLSI FQDAMAADSR
LFKLAIQENK HVFEGLESLV DVAGGTGGVA KLIHEAFPHI KCTVFDQPQV VGNLTGNENL
NFVSGDMFKS VPSADAVLLK WVLHDWNDEL SLKILKKSKE AISHKGKDGK VIIIDISIDD
NSDDHGLTEL QLEYDVVMLT MFLGKERTKK EWEKLIYDAG FSRYKITPIC GFKSLIEVYP
