ID   BMT_AMMMJ               Reviewed;         354 AA.
AC   Q6T1F6;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Bergaptol O-methyltransferase {ECO:0000312|EMBL:AAR24096.2};
DE            Short=BMT {ECO:0000303|PubMed:15009205};
DE            EC=2.1.1.69;
GN   Name=BMT {ECO:0000303|PubMed:15009205};
OS   Ammi majus (Bishop's weed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Ammi.
OX   NCBI_TaxID=48026;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAR24096.2}
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX   PubMed=15009205; DOI=10.1111/j.1432-1033.2004.03995.x;
RA   Hehmann M., Lukacin R., Ekiert H., Matern U.;
RT   "Furanocoumarin biosynthesis in Ammi majus L. Cloning of bergaptol O-
RT   methyltransferase.";
RL   Eur. J. Biochem. 271:932-940(2004).
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:15009205};
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:15009205};
CC   -!- ACTIVITY REGULATION: Inhibited by Cu(2+), Ni(2+) and Co(2+).
CC       {ECO:0000269|PubMed:15009205}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 uM for bergaptol {ECO:0000269|PubMed:15009205};
CC         KM=6.5 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:15009205};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:15009205};
CC       Temperature dependence:
CC         Optimum temperature is 42 degrees Celsius.
CC         {ECO:0000269|PubMed:15009205};
CC   -!- INDUCTION: Up-regulated by Pmg elicitor. {ECO:0000269|PubMed:15009205}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY443006; AAR24096.2; -; mRNA.
DR   AlphaFoldDB; Q6T1F6; -.
DR   SMR; Q6T1F6; -.
DR   KEGG; ag:AAR24096; -.
DR   BRENDA; 2.1.1.69; 296.
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..354
FT                   /note="Bergaptol O-methyltransferase"
FT                   /id="PRO_0000401110"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P28002,
FT                   ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         198
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         221
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         242
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         255
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   354 AA;  38727 MW;  60607D866758BC42 CRC64;
     MAEMKTSPSQ DEEAGVVAMQ LATSTVLPMI LKSAIELDLL NTIAKAGPGN YLSPSDLASK
     LLLSNPDAPV MLARILRVLA TYKVLGCKRG EVEWLYCWTP VCKYLSNNED GASIAPILLV
     HQDKVTIKSW YHLTDAVRDG GTAFNKAHDM SIFEYASQDP QFNKAFNRSM RGHSTITMKK
     ILETYKGFEG LKSIVDVGGG TGATLNMIIS KYPTIKGINF DLPHVVGDAP SLPGVEHVGG
     NMFASVPKGD AIFLKWIFHS WGDEECLKIL KKCHQALGDN KKVIVAEFIL PEDPGGSDSA
     TKSAVHLDAI MLAYVPGGKE RTEKEFESLA KRAGFKSFTK VCCAFNTWIM EFSK