BSMT1_PETHY
ID BSMT1_PETHY Reviewed; 357 AA.
AC Q84UB5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=S-adenosyl-L-methionine:benzoic acid/salicylic acid carboxyl methyltransferase 1 {ECO:0000303|PubMed:14630969};
DE Short=PhBSMT1 {ECO:0000303|PubMed:14630969};
DE EC=2.1.1.273 {ECO:0000269|PubMed:14630969};
DE EC=2.1.1.274 {ECO:0000269|PubMed:14630969};
GN Name=BSMT1 {ECO:0000303|PubMed:14630969};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, REPRESSION BY
RP POLLINATION AND ETHYLENE, AND PATHWAY.
RC STRAIN=cv. Mitchell;
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).
RN [2]
RP INDUCTION BY EOBI.
RC STRAIN=cv. W115;
RX PubMed=23275577; DOI=10.1105/tpc.112.105247;
RA Spitzer-Rimon B., Farhi M., Albo B., Cna'ani A., Ben Zvi M.M., Masci T.,
RA Edelbaum O., Yu Y., Shklarman E., Ovadis M., Vainstein A.;
RT "The R2R3-MYB-like regulatory factor EOBI, acting downstream of EOBII,
RT regulates scent production by activating ODO1 and structural scent-related
RT genes in petunia.";
RL Plant Cell 24:5089-5105(2012).
CC -!- FUNCTION: Converts benzoic acid into the volatile ester methyl
CC benzoates (PubMed:14630969). This scent, mostly produced in a
CC rhythmical, diurnal manner, attracts the pollinators (PubMed:14630969).
CC {ECO:0000269|PubMed:14630969}.
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:14630969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36100;
CC Evidence={ECO:0000269|PubMed:14630969};
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:14630969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36096;
CC Evidence={ECO:0000269|PubMed:14630969};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.93 uM for S-adenosyl-L-methionine (in the presence of salicylic
CC acid) {ECO:0000269|PubMed:14630969};
CC KM=15.78 uM for S-adenosyl-L-methionine (in the presence of benzoic
CC acid) {ECO:0000269|PubMed:14630969};
CC KM=51.55 uM for salicylic acid {ECO:0000269|PubMed:14630969};
CC KM=1273.2 uM for benzoic acid {ECO:0000269|PubMed:14630969};
CC Note=kcat is 0.0145 sec(-1) with S-adenosyl-L-methionine (in the
CC presence of salicylic acid) (PubMed:14630969). kcat is 0.0075 sec(-1)
CC with S-adenosyl-L-methionine (in the presence of benzoic acid)
CC (PubMed:14630969). kcat is 0.012 sec(-1) with salicylic acid as
CC substrate (PubMed:14630969). kcat is 0.0039 sec(-1) with benzoic acid
CC as substrate (PubMed:14630969). {ECO:0000269|PubMed:14630969};
CC pH dependence:
CC Optimum pH is 7-8 with salicylic acid as substrate (PubMed:14630969).
CC Optimum pH is 7.5 with benzoic acid as substrate (PubMed:14630969).
CC {ECO:0000269|PubMed:14630969};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:14630969}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in petal limbs and tubes of
CC corollas. {ECO:0000269|PubMed:14630969}.
CC -!- INDUCTION: Triggered by EOBI in flowers (PubMed:23275577). Fades out in
CC flower petals after pollination, thus resulting in a decrease in
CC methylbenzoate emission (PubMed:14630969). Strongly repressed by
CC ethylene (PubMed:14630969). {ECO:0000269|PubMed:14630969,
CC ECO:0000269|PubMed:23275577}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AY233465; AAO45012.1; -; mRNA.
DR AlphaFoldDB; Q84UB5; -.
DR SMR; Q84UB5; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
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 Magnesium; Metal-binding; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..357
FT /note="S-adenosyl-L-methionine:benzoic acid/salicylic acid
FT carboxyl methyltransferase 1"
FT /id="PRO_0000451511"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 21..25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 58..60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 58..59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 94..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 135..137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 152..154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 153..157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9SPV4"
SQ SEQUENCE 357 AA; 40662 MW; 6158315CDF0077EB CRC64;
MEVVEVLHMN GGNGDSSYAN NSLVQQKVIL MTKPITEQAM IDLYSSLFPE TLCIADLGCS
LGANTFLVVS QLVKIVEKER KKHGFKSPEF YFHFNDLPGN DFNTLFQSLG AFQEDLRKHI
GESFGPCFFS GVPGSFYTRL FPSKSLHFVY SSYSLMWLSQ VPNGIENNKG NIYMARTSPL
SVIKAYYKQY EIDFSNFLKY RSEELMKGGK MVLTLLGRES EDPTSKECCY IWELLAMALN
KLVEEGLIKE EKVDAFNIPQ YTPSPAEVKY IVEKEGSFTI NRLETSRVHW NASNNEKNGG
YNVSRCMRAV AEPLLVSHFD KELMDLVFHK YEEIVSDCMS KENTEFINVI ISLTKIN
