AAMT3_MAIZE
ID AAMT3_MAIZE Reviewed; 379 AA.
AC D9J100;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Anthranilate O-methyltransferase 3;
DE EC=2.1.1.277;
DE AltName: Full=Anthranilic acid methyltransferase 3;
DE AltName: Full=Benzoate O-methyltransferase;
DE EC=2.1.1.273;
DE AltName: Full=O-methyltransferase 3;
DE AltName: Full=Salicylate O-methyltransferas;
DE EC=2.1.1.274;
GN Name=AAMT3; Synonyms=OMT3;
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).
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. Can also use
CC benzoic acid as substrate. Low activity with salicylic acid.
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 -!- 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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + salicylate = methyl salicylate + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:36095, ChEBI:CHEBI:30762,
CC ChEBI:CHEBI:31832, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.274; Evidence={ECO:0000269|PubMed:20519632};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:20519632};
CC -!- INDUCTION: Up-regulated by herbivory and jasmonic acid, but not by
CC 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; HM242247; ADI87452.1; -; mRNA.
DR RefSeq; NP_001182138.1; NM_001195209.1.
DR AlphaFoldDB; D9J100; -.
DR SMR; D9J100; -.
DR STRING; 4577.GRMZM2G063438_P01; -.
DR PRIDE; D9J100; -.
DR GeneID; 103637798; -.
DR KEGG; zma:103637798; -.
DR eggNOG; ENOG502QQVK; Eukaryota.
DR OrthoDB; 689338at2759; -.
DR BRENDA; 2.1.1.277; 6752.
DR SABIO-RK; D9J100; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; D9J100; baseline and differential.
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 Methyltransferase; Plant defense; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..379
FT /note="Anthranilate O-methyltransferase 3"
FT /id="PRO_0000423913"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 143..145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 43220 MW; C619878702417BE9 CRC64;
MPMRIERDLH MATGNGETSY TKNSRIQEKV MFQIKPVLEE ATRAAYSALL PQTMVVADLG
CSSGPNTLRF VSEVIGIIAR HCKEHDRRHD YPQLQFFLND LPGNDFNNLF LLIQQFNKSM
ARNHKGEAAE ALPPCYISGL PGSFYTRIFP SESVHLFHSL FSVHWHSQAS EQLKDTKNKC
LDIYITKNMP PSMVKLFQQQ FEKDFSLFLK LRYEELVSGG QMVLTFIGRK HEDVFTGESN
HLYGLLAQSL KSLVDEGLVE KEKLESFYLP IYSPSVGEVE AIVKQVGLFN MNHVKVFEIN
WDPYGDSEGD DVHDSIRSGE NVAKCLRAVM EPLVASQFGE HILDKLFKEY ARRVAKHLEN
EKTKHAILVL SIEKAIIHV
