BMT_PEUPR
ID BMT_PEUPR Reviewed; 359 AA.
AC A0A166U5H3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Bergaptol O-methyltransferase {ECO:0000303|PubMed:27252733};
DE Short=PpBMT {ECO:0000303|PubMed:27252733};
DE EC=2.1.1.69 {ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994};
GN Name=BMT {ECO:0000303|PubMed:27252733};
OS Peucedanum praeruptorum (Kitagawia praeruptora).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Selineae; Peucedanum.
OX NCBI_TaxID=312531;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY METHYL
RP JASMONATE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-171; MET-175;
RP ASP-226; HIS-264 AND LEU-312.
RX PubMed=27252733; DOI=10.3389/fpls.2016.00722;
RA Zhao Y., Wang N., Zeng Z., Xu S., Huang C., Wang W., Liu T., Luo J.,
RA Kong L.;
RT "Cloning, functional characterization, and catalytic mechanism of a
RT bergaptol O-methyltransferase from Peucedanum praeruptorum Dunn.";
RL Front. Plant Sci. 7:722-722(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30934718; DOI=10.3390/ijms20071533;
RA Zhao Y., Wang N., Sui Z., Huang C., Zeng Z., Kong L.;
RT "The molecular and structural basis of O-methylation reaction in coumarin
RT biosynthesis in Peucedanum praeruptorum Dunn.";
RL Int. J. Mol. Sci. 20:0-0(2019).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATES ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF LEU-122; HIS-126;
RP ILE-157; PHE-158; MET-175; TRP-261; SER-265; LEU-312; VAL-315; MET-316;
RP TYR-319 AND VAL-320, BIOTECHNOLOGY, AND HOMODIMERIZATION.
RX PubMed=31666994; DOI=10.1016/j.jare.2019.10.003;
RA Zhao Y., Wang N., Wu H., Zhou Y., Huang C., Luo J., Zeng Z., Kong L.;
RT "Structure-based tailoring of the first coumarins-specific bergaptol O-
RT methyltransferase to synthesize bergapten for depigmentation disorder
RT treatment.";
RL J. Adv. Res. 21:57-64(2020).
CC -!- FUNCTION: O-methyltransferase involved in the biosynthesis of
CC furocoumarins natural products such as bergapten, a photosensitizer
CC used for medical purpose such as treating psoriasis and vitiligo or
CC facilitating resistance to microbial infection and other stresses
CC (PubMed:30934718, PubMed:27252733, PubMed:31666994). Catalyzes
CC specifically the methylation of bergaptol (PubMed:30934718,
CC PubMed:27252733, PubMed:31666994). Not active on xanthotol,
CC isoscopoletin, scopoletin and esculetin (PubMed:30934718,
CC PubMed:27252733). {ECO:0000269|PubMed:27252733,
CC ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.
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:27252733, ECO:0000269|PubMed:30934718,
CC ECO:0000269|PubMed:31666994};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11809;
CC Evidence={ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718,
CC ECO:0000269|PubMed:31666994};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:27252733,
CC ECO:0000269|PubMed:30934718, ECO:0000269|PubMed:31666994}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:27252733, ECO:0000269|PubMed:30934718,
CC ECO:0000269|PubMed:31666994}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31666994}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27252733}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and, to a lower extent,
CC in stems and leaves. {ECO:0000269|PubMed:27252733}.
CC -!- INDUCTION: Induced by methyl jasmonate (MeJA).
CC {ECO:0000269|PubMed:27252733}.
CC -!- BIOTECHNOLOGY: The high-activity Ile-320 mutant could be used in
CC metabolic engineering to produce bergapten in order to treat
CC depigmentation disorder. {ECO:0000303|PubMed:31666994}.
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, ECO:0000305}.
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DR EMBL; KU359196; ANA75355.1; -; mRNA.
DR PDB; 5XOH; X-ray; 2.20 A; A=1-359.
DR PDBsum; 5XOH; -.
DR SMR; A0A166U5H3; -.
DR BRENDA; 2.1.1.69; 15750.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030752; F:5-hydroxyfuranocoumarin 5-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009805; P:coumarin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
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 3D-structure; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..359
FT /note="Bergaptol O-methyltransferase"
FT /id="PRO_0000454878"
FT REGION 157..175
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:31666994,
FT ECO:0007744|PDB:5XOH"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000269|PubMed:31666994, ECO:0007744|PDB:5XOH"
FT BINDING 125..131
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31666994,
FT ECO:0007744|PDB:5XOH"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31666994,
FT ECO:0007744|PDB:5XOH"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000269|PubMed:31666994, ECO:0007744|PDB:5XOH"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31666994,
FT ECO:0007744|PDB:5XOH"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31666994,
FT ECO:0007744|PDB:5XOH"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31666994,
FT ECO:0007744|PDB:5XOH"
FT SITE 126
FT /note="Determines the catalytic selectivity of hydroxyl
FT groups in esculetin"
FT /evidence="ECO:0000250|UniProtKB:A0A4P8DY91"
FT MUTAGEN 122
FT /note="L->F: Slightly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 122
FT /note="L->H: Reduced catalytic activity. Strongly reduced
FT catalytic activity; when associated with H-261. Strongly
FT reduced catalytic activity; when associated with F-126 and
FT H-261."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 122
FT /note="L->R: Abolished catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 126
FT /note="H->F: Strongly reduced catalytic activity; when
FT associated with H-122 and H-261."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 157
FT /note="I->F: Increased catalytic activity; when associated
FT with I-320."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 157
FT /note="I->H: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 157
FT /note="I->Y: Increased catalytic activity. Slightly
FT increased catalytic activity; when associated with N-265.
FT Strongly reduced catalytic activity; when associated with
FT F-265 and N-315."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 158
FT /note="F->Y: Abolished catalytic activity; when associated
FT with P-265 and Q-315."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 171
FT /note="F->A: Altered substrate binding."
FT /evidence="ECO:0000269|PubMed:27252733"
FT MUTAGEN 175
FT /note="M->A: Altered substrate binding."
FT /evidence="ECO:0000269|PubMed:27252733"
FT MUTAGEN 175
FT /note="M->Y: Abolished catalytic activity; when associated
FT with W-316."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 226
FT /note="D->A: Altered substrate binding."
FT /evidence="ECO:0000269|PubMed:27252733"
FT MUTAGEN 261
FT /note="W->H: Slightly increased catalytic activity.
FT Strongly reduced catalytic activity; when associated with
FT H-122. Strongly reduced catalytic activity; when associated
FT with H-122 and F-126."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 261
FT /note="W->K: Abolished catalytic activity; when associated
FT with Y-316."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 261
FT /note="W->L: Normal catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 264
FT /note="H->A: Altered catalytic activity."
FT /evidence="ECO:0000269|PubMed:27252733"
FT MUTAGEN 265
FT /note="S->F: Strongly reduced catalytic activity; when
FT associated with Y-157 and N-315. Abolished catalytic
FT activity; when associated with N-315 and I-320."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 265
FT /note="S->H: Abolished catalytic activity; when associated
FT with N-315."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 265
FT /note="S->I: Increased catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 265
FT /note="S->N: Slightly increased catalytic activity.
FT Slightly increased catalytic activity; when associated with
FT Y-157."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 265
FT /note="S->P: Abolished catalytic activity; when associated
FT with Y-158 and Q-315."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 312
FT /note="L->A: Altered substrate binding."
FT /evidence="ECO:0000269|PubMed:27252733"
FT MUTAGEN 315
FT /note="V->F: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 315
FT /note="V->N: Abolished catalytic activity; when associated
FT with H-265. Strongly reduced catalytic activity; when
FT associated with Y-157 and F-265. Abolished catalytic
FT activity; when associated with F-265 and I-320."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 315
FT /note="V->Q: Abolished catalytic activity; when associated
FT with Y-158 and P-265."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 316
FT /note="M->W: Abolished catalytic activity; when associated
FT with Y-175."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 316
FT /note="M->Y: Abolished catalytic activity; when associated
FT with K-261."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 319
FT /note="Y->F: Strongly increased catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 319
FT /note="Y->R: Abolished catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 320
FT /note="V->I: Strongly increased catalytic activity.
FT Increased catalytic activity; when associated with F-157.
FT Abolished catalytic activity; when associated with F-265
FT and N-315."
FT /evidence="ECO:0000269|PubMed:31666994"
FT MUTAGEN 320
FT /note="V->Y: Slightly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:31666994"
FT HELIX 9..22
FT /evidence="ECO:0007829|PDB:5XOH"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 165..186
FT /evidence="ECO:0007829|PDB:5XOH"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:5XOH"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5XOH"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:5XOH"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5XOH"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5XOH"
SQ SEQUENCE 359 AA; 39269 MW; 962E403762A65817 CRC64;
MAGMKTSPSQ DEEACVLAIQ LATSTVLPMI LKSAIELDIL NTISKAGPGN YLSPSDLASK
LLMSNPHAPI MLERILRVLA TYKVLGCKPS ELSDGEVEWL YCWTPVCKFL SNNEDGASIA
PLLLVHQDQV PMKSWYHLTD AILDGGTAFN KAYGMNIFDY ASQDPQFNKV FNRSMAGHST
ITMKKILETY NGFEGLKSIV DVGGGSGATL NMIISKYPTI KGINFDLPHV VGDSPIHPGV
EHVGGDMFAS VPKGDAIFLK WIFHSWSDED CLRILKNCYE ALADNKKVIV AEFIIPEVPG
GSDDATKSVV HLDAVMLAYV PGGKERTEKE FEALATSAGF KSFRKVCCAF NTWIMEFSK
