ID   OMT8_MAIZE              Reviewed;         385 AA.
AC   D9J101;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Benzoate O-methyltransferase;
DE            EC=2.1.1.273;
DE   AltName: Full=O-methyltransferase 8;
GN   Name=OMT8;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Delprim;
RX   PubMed=20519632; DOI=10.1104/pp.110.158360;
RA   Kollner T.G., Lenk C., Zhao N., Seidl-Adams I., Gershenzon J., Chen F.,
RA   Degenhardt J.;
RT   "Herbivore-induced SABATH methyltransferases of maize that methylate
RT   anthranilic acid using s-adenosyl-L-methionine.";
RL   Plant Physiol. 153:1795-1807(2010).
CC   -!- FUNCTION: Methyltransferase involved in the biosynthesis of methyl
CC       benzoate in response to stresses. Utilizes exclusively benzoic acid
CC       (BA) as substrate. {ECO:0000269|PubMed:20519632}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzoate + S-adenosyl-L-methionine = methyl benzoate + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:36099, ChEBI:CHEBI:16150,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:72775;
CC         EC=2.1.1.273; Evidence={ECO:0000269|PubMed:20519632};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC       methyltransferase family. SABATH subfamily. {ECO:0000305}.
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DR   EMBL; HM242248; ADI87453.1; -; mRNA.
DR   RefSeq; NP_001182139.1; NM_001195210.1.
DR   AlphaFoldDB; D9J101; -.
DR   SMR; D9J101; -.
DR   STRING; 4577.GRMZM2G126772_P01; -.
DR   PaxDb; D9J101; -.
DR   PRIDE; D9J101; -.
DR   GeneID; 113604963; -.
DR   eggNOG; ENOG502QQVK; Eukaryota.
DR   OrthoDB; 689338at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; D9J101; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0080150; F:S-adenosyl-L-methionine:benzoic acid carboxyl methyl transferase activity; IEA:RHEA.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IBA:GO_Central.
DR   Gene3D; 1.10.1200.270; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR005299; MeTrfase_7.
DR   InterPro; IPR042086; MeTrfase_capping.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR31009; PTHR31009; 1.
DR   Pfam; PF03492; Methyltransf_7; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Methyltransferase; Plant defense;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..385
FT                   /note="Benzoate O-methyltransferase"
FT                   /id="PRO_0000423914"
FT   BINDING         18
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..60
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         145..147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  43586 MW;  62AC8BFB3B26394F CRC64;
     MDIRRDFHMA EGEGEWSYSK NCRRQQVAVR ETRPMVETAV KQVYAALLPR TMVVADLGCS
     AGPNTLLFIS SVLSSIAAAA AEQCKPPSGG GDDDDHHVEL QFVLNDLPGN DFNHLFRSVE
     EEFRRAAGCE RAPHPPYYVM GLPESYYNRL FPRQSVHLFH SSYCLQWRSQ EPEGLEAWRK
     PCLNEDNIYI ARTTTPSVAK LFQEQFQKDF SLFLKLRHEE LVHGGRMVLI FLGRKNEDVY
     SGDLNQLFAL VATALQSLVL KGLVEKEKLE SFNLPVYGPS VGEVEELVTR SGLQFSMDLI
     KQFEMNWDPF DDSEGDNDVV VVEDSARSSV NVAKLIRSVL KALVVRHFGE AVLDACFAEF
     RRLVAEHLGK EKTKFTTIAM CLKKE