BSMT3_PETHY
ID BSMT3_PETHY Reviewed; 357 AA.
AC A4ZDG8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=S-adenosyl-L-methionine:benzoic acid/salicylic acid carboxyl methyltransferase 3 {ECO:0000303|Ref.1};
DE Short=PhBSMT3 {ECO:0000303|Ref.1};
DE EC=2.1.1.273 {ECO:0000250|UniProtKB:Q84UB5};
GN Name=BSMT3 {ECO:0000303|Ref.1};
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].
RA Long Z., Yu L., Zhang H.;
RT "Cloning and expression identification of the S-adenosyl-L-
RT methionine:benzoic acid/salicylic acid carboxyl methyltransferase for
RT Petunia x hybrida.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts benzoic acid into the volatile ester methyl
CC benzoates (By similarity). This scent, mostly produced in a rhythmical,
CC diurnal manner, attracts the pollinators (By similarity).
CC {ECO:0000250|UniProtKB:Q84UB5}.
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:0000250|UniProtKB:Q84UB5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36100;
CC Evidence={ECO:0000250|UniProtKB:Q84UB5};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000250|UniProtKB:Q84UB5}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; DQ494491; ABF50941.1; -; mRNA.
DR AlphaFoldDB; A4ZDG8; -.
DR SMR; A4ZDG8; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; ISS: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 2: Evidence at transcript 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 3"
FT /id="PRO_0000451513"
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; 40646 MW; 5F7603D8BFB886F8 CRC64;
MEVVEVLHMN GGNGDSSYAN NSLVQQKVIL MTKPITEQAM IDLYSSLFPE TLCIADLGCS
LGANTFLVVS QIVKIVEKER KKHGFKSPEF YFHFNDLPGN DFNTLFQSLG AFQEDLRKHI
GESFGPCFFS GVPGSFYTRL FPSKSLHFVY SSYSLMWLSQ VPNGIENNKG NIYMARTSPL
SVIKAYYKQY EIDFSNFLKY RSEELMKGGK MVLTLLGRES EDPTSKECCY IWELLAMALN
ELVKEGLIKE EKVDAFNIPQ YTPSPAEVKY LVEKEGSFTI NRLETSRVHW NASNNVKNGG
YNVSRCMRAV AEPLLVSHFD KELMDLVFHK YEEIISDCMS KEKTEFINVI VSLTKIN
