AAMT1_MAIZE
ID AAMT1_MAIZE Reviewed; 382 AA.
AC D9J0Z7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Anthranilate O-methyltransferase 1;
DE EC=2.1.1.277;
DE AltName: Full=Anthranilic acid methyltransferase 1;
DE AltName: Full=O-methyltransferase 1;
GN Name=AAMT1; Synonyms=OMT1;
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, INDUCTION BY HERBIVORY; JASMONIC ACID AND
RP SALICYLIC ACID, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF GLN-167 AND
RP TYR-246.
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 anthranilate in response to stresses. Utilizes anthranilic acid as
CC substrate, but not salicylic acid. Produces exclusively the O-methyl
CC ester. {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=641 uM for anthranilic acid {ECO:0000269|PubMed:20519632};
CC KM=2025 uM for benzoic acid {ECO:0000269|PubMed:20519632};
CC KM=79 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:20519632};
CC Note=kcat is 0.45 sec(-1) with anthranilic acid as substrate. kcat is
CC 0.04 sec(-1) with benzoic acid as substrate.;
CC -!- INDUCTION: Up-regulated by herbivory and jasmonic acid, but not by
CC salicylic acid. {ECO:0000269|PubMed:20519632}.
CC -!- MISCELLANEOUS: Because cv. Delprim is a hybrid line, AAMT1 and AAMT1I
CC are likely alleles of one single locus. However, AAMT1I showed no
CC enzymatic activity with all tested substrates (PubMed:20519632).
CC {ECO:0000305|PubMed:20519632}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. SABATH subfamily. {ECO:0000305}.
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DR EMBL; HM242244; ADI87449.1; -; mRNA.
DR AlphaFoldDB; D9J0Z7; -.
DR SMR; D9J0Z7; -.
DR STRING; 4577.GRMZM2G039993_P01; -.
DR PaxDb; D9J0Z7; -.
DR PRIDE; D9J0Z7; -.
DR eggNOG; ENOG502QQVK; Eukaryota.
DR BRENDA; 2.1.1.277; 6752.
DR SABIO-RK; D9J0Z7; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; D9J0Z7; 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..382
FT /note="Anthranilate O-methyltransferase 1"
FT /id="PRO_0000423910"
FT BINDING 20
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60..62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 146..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 167
FT /note="Q->H: Increased activity with benzoic acid as
FT substrate, but no activity with salicylic acid as
FT substrate."
FT /evidence="ECO:0000269|PubMed:20519632"
FT MUTAGEN 167
FT /note="Q->M: No effect on substrate specificity."
FT /evidence="ECO:0000269|PubMed:20519632"
FT MUTAGEN 246
FT /note="Y->W: Decreased substrate specificity and increased
FT activity with benzoic acid and salicylic acid as
FT substrates."
FT /evidence="ECO:0000269|PubMed:20519632"
SQ SEQUENCE 382 AA; 43588 MW; 884A4AFFED227538 CRC64;
MPMRIERDLH MAIGNGETSY TKNSRIQEKA MFQMKSVLEE ATRAVCTTLL PQTMVVADLG
CSSGPNTLRF VTEVTRIIAH HCKLEHNRRH DHLPQLQFFL NDLPGNDFNN LFQLIEQFNK
SSTTHKGDAA TEALQPPCYI SGLPGSYYTR IFPSESVHLF HSLFCLQWRS QAPEQLKGTQ
KSCLDIYITK TMSPSMVKLF QQQFQKDFSL FLRLRYEELV SGGQMVLTFI GRKHEDVFTG
ESNHLYGLLA QSLKSLVDEG LVEKEKLESF YLPIYSPSVG EVEAIVKQLG LFNMNHVKVF
EINWDPYDDS EGDDVHNSIE SGENVAKCLR AVMEPLVASQ FGERILDELF KEYARRVAKH
LENEKTKHAV LVLSIEKAII HV
