BAMT_ANTMA
ID BAMT_ANTMA Reviewed; 364 AA.
AC Q9FYZ9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Benzoate carboxyl methyltransferase {ECO:0000303|PubMed:10852939};
DE EC=2.1.1.273 {ECO:0000269|PubMed:10852939};
DE AltName: Full=S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase {ECO:0000303|PubMed:10852939};
GN Name=BAMT {ECO:0000303|PubMed:10852939};
OS Antirrhinum majus (Garden snapdragon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=4151;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=10852939; DOI=10.2307/3871221;
RA Dudareva N., Murfitt L.M., Mann C.J., Gorenstein N., Kolosova N.,
RA Kish C.M., Bonham C., Wood K.;
RT "Developmental regulation of methyl benzoate biosynthesis and emission in
RT snapdragon flowers.";
RL Plant Cell 12:949-961(2000).
RN [2]
RP TISSUE SPECIFICITY, AND REPRESSION BY POLLINATION AND ETHYLENE.
RC STRAIN=cv. Maryland True Pink;
RX PubMed=14630969; DOI=10.1105/tpc.016766;
RA Negre F., Kish C.M., Boatright J., Underwood B., Shibuya K., Wagner C.,
RA Clark D.G., Dudareva N.;
RT "Regulation of methylbenzoate emission after pollination in snapdragon and
RT petunia flowers.";
RL Plant Cell 15:2992-3006(2003).
CC -!- FUNCTION: Converts benzoic acid into the volatile ester methyl
CC benzoates. This scent, mostly produced in a rhythmical, diurnal manner,
CC attracts the pollinators. {ECO:0000269|PubMed:10852939}.
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:10852939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36100;
CC Evidence={ECO:0000269|PubMed:10852939};
CC -!- TISSUE SPECIFICITY: Expressed only in the upper and lower petal lobes
CC (PubMed:10852939, PubMed:14630969). Not found in the corolla tubes,
CC anthers, pistils, sepals and ovaries (PubMed:10852939).
CC {ECO:0000269|PubMed:10852939, ECO:0000269|PubMed:14630969}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mature flowers with a peak 6 to 7
CC days postanthesis. {ECO:0000269|PubMed:10852939}.
CC -!- INDUCTION: Fades out in flower petals after pollination, thus resulting
CC in a decrease in methylbenzoate emission (PubMed:14630969). Strongly
CC repressed by ethylene (PubMed:14630969). {ECO:0000269|PubMed:14630969}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AF198492; AAF98284.1; -; mRNA.
DR AlphaFoldDB; Q9FYZ9; -.
DR SMR; Q9FYZ9; -.
DR KEGG; ag:AAF98284; -.
DR BRENDA; 2.1.1.273; 376.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
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 Direct protein sequencing; Magnesium; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..364
FT /note="Benzoate carboxyl methyltransferase"
FT /id="PRO_0000204466"
FT BINDING 20
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 23..27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 62..64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 62..63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 99..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 129..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 146..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 147..151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
SQ SEQUENCE 364 AA; 41011 MW; C10C8E864A581419 CRC64;
MKVMKKLLCM NIAGDGETSY ANNSGLQKVM MSKSLHVLDE TLKDIIGDHV GFPKCFKMMD
MGCSSGPNAL LVMSGIINTI EDLYTEKNIN ELPEFEVFLN DLPDNDFNNL FKLLSHENGN
CFVYGLPGSF YGRLLPKKSL HFAYSSYSIH WLSQVPEGLE DNNRQNIYMA TESPPEVYKA
YAKQYERDFS TFLKLRGEEI VPGGRMVLTF NGRSVEDPSS KDDLAIFTLL AKTLVDMVAE
GLVKMDDLYS FNIPIYSPCT REVEAAILSE GSFTLDRLEV FRVCWDASDY TDDDDQQDPS
IFGKQRSGKF VADCVRAITE PMLASHFGST IMDLLFGKYA KKIVEHLSVE NSSYFSIVVS
LSRR
