ID   AAMT2_MAIZE             Reviewed;         374 AA.
AC   B6SU46;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Anthranilate O-methyltransferase 2;
DE            EC=2.1.1.277;
DE   AltName: Full=Anthranilic acid methyltransferase 2;
DE   AltName: Full=Benzoate carboxyl methyltransferase;
DE   AltName: Full=O-methyltransferase 2;
GN   Name=AAMT2; Synonyms=OMT2;
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, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY HERBIVORY; JASMONIC ACID
RP   AND SALICYLIC ACID.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
CC   -!- FUNCTION: Methyltransferase involved in the biosynthesis of methyl
CC       anthranilate in response to stresses. Utilizes anthranilic acid as
CC       substrate. Produces exclusively the O-methyl ester.
CC       {ECO:0000269|PubMed:20519632}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=anthranilate + S-adenosyl-L-methionine = O-methyl anthranilate
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36103, ChEBI:CHEBI:16567,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73244;
CC         EC=2.1.1.277; Evidence={ECO:0000269|PubMed:20519632};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=311 uM for anthranilic acid {ECO:0000269|PubMed:20519632};
CC         KM=94 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:20519632};
CC         Note=kcat is 0.37 sec(-1) with anthranilic acid as substrate.;
CC   -!- INDUCTION: Slightly up-regulated by herbivory and jasmonic acid, but
CC       not by salicylic acid. {ECO:0000269|PubMed:20519632}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC       methyltransferase family. SABATH subfamily. {ECO:0000305}.
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DR   EMBL; HM242246; ADI87451.1; -; mRNA.
DR   EMBL; EU956261; ACG28379.1; -; mRNA.
DR   RefSeq; NP_001147683.1; NM_001154211.1.
DR   AlphaFoldDB; B6SU46; -.
DR   SMR; B6SU46; -.
DR   STRING; 4577.GRMZM2G116966_P01; -.
DR   PaxDb; B6SU46; -.
DR   PRIDE; B6SU46; -.
DR   GeneID; 100281293; -.
DR   eggNOG; ENOG502QQVK; Eukaryota.
DR   OrthoDB; 689338at2759; -.
DR   BRENDA; 2.1.1.277; 6752.
DR   SABIO-RK; B6SU46; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; B6SU46; baseline and differential.
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   Methyltransferase; Plant defense; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..374
FT                   /note="Anthranilate O-methyltransferase 2"
FT                   /id="PRO_0000423912"
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         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..144
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  42666 MW;  23989DE46CC0F004 CRC64;
     MRIERDLHMA TGDGETSYTK NSRIQEKTMF QIKPVLEEAT RAVYTALHPQ TMVVADLGCS
     SGPNTLRFVS EVIGIIARHC KEYGRQHDHT QLQFFLNDLP GNDFNNLFQL IQQFNKSTAI
     NHKSEAAEAL PPPCYISGLP GSYYTRIFPS ESVHLFHSLF CLQWRSEAPE GNKKTCLDIY
     ITKTMSPSMV KLFQQQFQKD FSLFLRLRYE ELVSGGQMVL TFIGRKHENV FTGESNHLYG
     LLAQSLKSLV DEGLVEKEKL ESFYLPMYSP SVGEVEAILK QVGLFNMNHV KVFQTNWDPY
     DDLESDVVHN SIRSGENVAK CLRAVMQPLV ASQFGEPILD KLFKEYARRV AKHLENEKTK
     HAIIVLSIEK AIHL