AAM1I_MAIZE
ID AAM1I_MAIZE Reviewed; 382 AA.
AC D9J0Z8;
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=Inactive anthranilate O-methyltransferase 1;
DE AltName: Full=Anthranilic acid methyltransferase 1;
DE AltName: Full=O-methyltransferase 1;
GN Name=AAMT1I; Synonyms=OMT1B;
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].
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 -!- 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; HM242245; ADI87450.1; -; mRNA.
DR RefSeq; NP_001182137.1; NM_001195208.1.
DR AlphaFoldDB; D9J0Z8; -.
DR SMR; D9J0Z8; -.
DR PRIDE; D9J0Z8; -.
DR GeneID; 100500707; -.
DR KEGG; zma:100500707; -.
DR OrthoDB; 689338at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; D9J0Z8; baseline and differential.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..382
FT /note="Inactive anthranilate O-methyltransferase 1"
FT /id="PRO_0000423911"
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"
SQ SEQUENCE 382 AA; 43548 MW; 6B717687570FAA62 CRC64;
MPMRIERDLH MAIGNGETSY TKNSRIQEKA MFQMKSVLEE ATRAVCTTLL PQTMVVADLG
CSSGPNTLRF VTEVTRIIAH HCKLEHNRRH DHLPQLQFFL NDLPGNDFNN LFQLIEQFNK
SSTTHKGDAA TEALQPPCYI SGLPGSYYTR IFSSESVHLF HSLFCLQWRS QAPEQLKGTQ
KSCLDIYITK AMSPSMVKLF QQQFQKDFSL FLRLRYEELV SGGQMVLTFI GRKHEDVFTG
ESNHLYGLLA QSLKSLVDEG LVEKEKLESF YLPIYSPSVG EVEAIVKQLG LFNMNHVKVF
EINWDPYDDS EGDDVHNSIE SGENVAKCLR AVMEPLVASQ FGERILDELF KEYARRVAKH
LENEKTKHAV LVLSIEKAII HV
