ID   BMT_GLELI               Reviewed;         359 AA.
AC   A8J6X1;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Bergaptol O-methyltransferase {ECO:0000312|EMBL:BAF81987.1};
DE            Short=BMT {ECO:0000303|PubMed:18974989};
DE            EC=2.1.1.69;
GN   Name=BMT {ECO:0000312|EMBL:BAF81987.1};
OS   Glehnia littoralis (Beach silvertop) (Phellopterus littoralis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Selineae; Glehnia.
OX   NCBI_TaxID=48119;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAF81987.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND INDUCTION.
RX   PubMed=18974989; DOI=10.1007/s00299-008-0631-9;
RA   Ishikawa A., Kuma T., Sasaki H., Sasaki N., Ozeki Y., Kobayashi N.,
RA   Kitamura Y.;
RT   "Constitutive expression of bergaptol O-methyltransferase in Glehnia
RT   littoralis cell cultures.";
RL   Plant Cell Rep. 28:257-265(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5-hydroxyfurocoumarin + S-adenosyl-L-methionine = a 5-
CC         methoxyfurocoumarin + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:18861, ChEBI:CHEBI:15378, ChEBI:CHEBI:52058,
CC         ChEBI:CHEBI:52061, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.69;
CC         Evidence={ECO:0000269|PubMed:18974989};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bergaptol + S-adenosyl-L-methionine = bergapten + S-adenosyl-
CC         L-homocysteine; Xref=Rhea:RHEA:11808, ChEBI:CHEBI:18293,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77728; EC=2.1.1.69;
CC         Evidence={ECO:0000269|PubMed:18974989};
CC   -!- ACTIVITY REGULATION: Inhibited by Cu(2+), Ni(2+) and Co(2+).
CC       {ECO:0000250|UniProtKB:Q6T1F6}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.9 uM for bergaptol {ECO:0000269|PubMed:18974989};
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:18974989}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; AB363638; BAF81987.1; -; mRNA.
DR   AlphaFoldDB; A8J6X1; -.
DR   SMR; A8J6X1; -.
DR   GO; GO:0030752; F:5-hydroxyfuranocoumarin 5-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..359
FT                   /note="Bergaptol O-methyltransferase"
FT                   /id="PRO_0000401111"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P28002,
FT                   ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002,
FT                   ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002,
FT                   ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         246
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002,
FT                   ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         247
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002,
FT                   ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002,
FT                   ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   359 AA;  39384 MW;  310E60371E4BEBFF CRC64;
     MAGMKSSPSQ DEEACVLAIQ LATSTVLPMI LKSAIELDIL NTISKAGPGN YLSPSDLASK
     LLMSNPHAPI MLERILRVLA TYKVLGCKRS ELSNGEVEWL YCWTPVCKFL SNNEDGASIA
     PLLLVHQDKV PMKSWYHLTD AVLDGGTAFN KAYGMNIFDY ASQDPQFNKV FNRSMAGHST
     ITMKKIVETY NGFEGLKSIV DVGGGSGATL NMIISKYPTI KGINFDLPHV VGDSPIHPGV
     EHVGGDMFAS VPKGDAIFLK WIFHSWSDED CLRILKNCYE ALADNKKVIV AEFIIPEVPG
     GSDDATKSVV HLDAIMLAYV PGGKERTEKE FESLATRAGF KSFRKVCCAF NTWIMEFSK