DOMT1_SINHE
ID DOMT1_SINHE Reviewed; 349 AA.
AC A0A0N9HTA1;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Desmethyl-yatein O-methyltransferase {ECO:0000303|PubMed:26359402};
DE EC=2.1.1.330 {ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000269|PubMed:26359402};
GN Name=OMT1 {ECO:0000303|PubMed:26359402};
GN Synonyms=Phex13114 {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, INDUCTION BY WOUNDING, 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 (-)-5'-
CC demethylyatein to produce (-)-yatein (PubMed:26359402).
CC {ECO:0000269|PubMed:26359402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:49040,
CC ChEBI:CHEBI:4553, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90894; EC=2.1.1.330;
CC Evidence={ECO:0000269|PubMed:26359402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49041;
CC Evidence={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}.
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; KT390155; ALG05117.1; -; mRNA.
DR AlphaFoldDB; A0A0N9HTA1; -.
DR SMR; A0A0N9HTA1; -.
DR KEGG; ag:ALG05117; -.
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..349
FT /note="Desmethyl-yatein O-methyltransferase"
FT /id="PRO_0000451905"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 282
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 314
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 193..194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 236..237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 236
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:0000250|UniProtKB:P28002"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 250
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
SQ SEQUENCE 349 AA; 38175 MW; EF3BB96625D6E7D8 CRC64;
MDTRADAEIK AMELIGIGVL PLAMKAIIEL NVLEILSKAG PDTQLTAAQI VTDIPTTNPN
AGFQLDRILR LLASHSVLSS SITKSGERVY GLTPMCKYFL PDQDGVSLAP MVVTIHDKVL
LQSWHYLKDS VLKQGSLPFT EAFGMSPFEY SVSDTRFNKV FNAGMFDHST LCMRDVLQRY
KGFQGLGELV DVGGGTGGSL KMILSQYPNL KGINFDLPHV VADAPSFPGV KHIGGDMFES
VPSGDAIFMK WILHDWDDGR CLTLLKNCWN ALPEHGKVII VEWILPSDAA TDPTSRRVFT
ADLMMLAFSE GGKERTLGDY GALAKEAGFT TVKDFPCANG ISVIEFHKK
