POMT3_SINHE
ID POMT3_SINHE Reviewed; 372 AA.
AC A0A0N9HMN6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Pluviatolide O-methyltransferase {ECO:0000303|PubMed:26359402};
DE Short=PhOMT3 {ECO:0000303|PubMed:26359402};
DE EC=2.1.1.323 {ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|PubMed:26359402};
GN Name=OMT3 {ECO:0000303|PubMed:26359402};
GN Synonyms=Phex2402 {ECO:0000303|PubMed:26359402};
OS Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Podophylloideae;
OC Sinopodophyllum.
OX NCBI_TaxID=93608;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY,
RP TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY WOUNDING,
RP AND PATHWAY.
RX PubMed=26359402; DOI=10.1126/science.aac7202;
RA Lau W., Sattely E.S.;
RT "Six enzymes from mayapple that complete the biosynthetic pathway to the
RT etoposide aglycone.";
RL Science 349:1224-1228(2015).
CC -!- FUNCTION: O-methyltransferase involved in the biosynthesis of
CC etoposide, a chemotherapeutic compound of the topoisomerase inhibitor
CC family (PubMed:26359402). Catalyzes the methylation of (-)-pluviatolide
CC to produce (-)-bursehernin (PubMed:26359402).
CC {ECO:0000269|PubMed:26359402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-pluviatolide + S-adenosyl-L-methionine = (-)-bursehernin +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49036,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90893, ChEBI:CHEBI:90896; EC=2.1.1.323;
CC Evidence={ECO:0000269|PubMed:26359402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49037;
CC Evidence={ECO:0000269|PubMed:26359402};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 uM for (-)-pluviatolide {ECO:0000269|PubMed:26359402};
CC Vmax=1.7 nmol/min/mg enzyme with (-)-pluviatolide as substrate
CC {ECO:0000269|PubMed:26359402};
CC Note=kcat is 0.72 sec(-1) with (-)-pluviatolide as substrate.
CC {ECO:0000269|PubMed:26359402};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:26359402}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28002}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, and, to a lower extent,
CC in leaves. {ECO:0000269|PubMed:26359402}.
CC -!- INDUCTION: Transiently induced after wounding.
CC {ECO:0000269|PubMed:26359402}.
CC -!- BIOTECHNOLOGY: Combinatorially expression of Sinopodophyllum hexandrum
CC (mayapple) genes of the podophyllotoxin pathway (e.g. DIR, PLR, SDH,
CC CYP719A23, OMT3, CYP71CU1, OMT1, 2-ODD, CYP71BE54 and CYP82D61) in
CC Nicotiana benthamiana (tobacco) results in the production of the
CC chemotherapeutic compound etoposide. {ECO:0000305|PubMed:26359402}.
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; KT390157; ALG05119.1; -; mRNA.
DR AlphaFoldDB; A0A0N9HMN6; -.
DR SMR; A0A0N9HMN6; -.
DR KEGG; ag:ALG05119; -.
DR BRENDA; 2.1.1.323; 4928.
DR UniPathway; UPA00711; -.
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:0032259; P:methylation; IDA:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; 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 Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..372
FT /note="Pluviatolide O-methyltransferase"
FT /id="PRO_0000451904"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 306
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 338
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 214..215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 214
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 257..258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
SQ SEQUENCE 372 AA; 41268 MW; 2A8E247A8A3B3274 CRC64;
MEMAPTMDLE IRNGNGYGDS GEELLAAQAH IYNHIFNFIS SMALKCAVEL NIPEILHNHQ
PKAVTLSELV QALQIPQAKS ACLYRLLRIL VHSGFFAITK IQSEGDEEGY LPTLSSKLLL
KNHPMSMSPC LLGLVNPTMV APMHFFSDWF KRSDDMTPFE ATHGASLWKY FGETPHMAEI
FNEAMGCETR LAMSVVLKEC KGKLEGISSL VDVGGGTGNV GRAIAEAFPN VKCTVLDLPQ
VVGNLKGSNN LEFVSGDMFQ FIPPADVVFL KWILHDWNDE ECIKILKRCK EAIPSKEEGG
KLIIIDMVVN DHNKGSYEST ETQLFYDLTL MALLTGTERT ETEWKKLFVA AGFTSYIISP
VLGLKSIIEV FP
