7OMT_PAPSO
ID 7OMT_PAPSO Reviewed; 355 AA.
AC Q6WUC2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=(R,S)-reticuline 7-O-methyltransferase {ECO:0000303|PubMed:14675446};
DE Short=7OMT {ECO:0000303|PubMed:14675446};
DE EC=2.1.1.291 {ECO:0000269|PubMed:14675446};
GN Name=7OMT {ECO:0000303|PubMed:15353584};
GN Synonyms=PSOMT1 {ECO:0000303|PubMed:14675446};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 185-199; 238-252; 285-299;
RP 321-325 AND 328-352, TISSUE SPECIFICITY, SUBUNIT, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14675446; DOI=10.1046/j.1365-313x.2003.01928.x;
RA Ounaroon A., Decker G., Schmidt J., Lottspeich F., Kutchan T.M.;
RT "(R,S)-Reticuline 7-O-methyltransferase and (R,S)-norcoclaurine 6-O-
RT methyltransferase of Papaver somniferum - cDNA cloning and characterization
RT of methyl transfer enzymes of alkaloid biosynthesis in opium poppy.";
RL Plant J. 36:808-819(2003).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15353584; DOI=10.1073/pnas.0405704101;
RA Weid M., Ziegler J., Kutchan T.M.;
RT "The roles of latex and the vascular bundle in morphine biosynthesis in the
RT opium poppy, Papaver somniferum.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13957-13962(2004).
RN [3]
RP FUNCTION.
RX PubMed=22725256; DOI=10.1111/j.1365-313x.2012.05084.x;
RA Desgagne-Penix I., Facchini P.J.;
RT "Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes
RT reveals the major route to papaverine in opium poppy.";
RL Plant J. 72:331-344(2012).
RN [4]
RP FUNCTION.
RX PubMed=23738019; DOI=10.1371/journal.pone.0065622;
RA Pathak S., Lakhwani D., Gupta P., Mishra B.K., Shukla S., Asif M.H.,
RA Trivedi P.K.;
RT "Comparative transcriptome analysis using high papaverine mutant of Papaver
RT somniferum reveals pathway and uncharacterized steps of papaverine
RT biosynthesis.";
RL PLoS ONE 8:E65622-E65622(2013).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group to reticuline to
CC form laudanine. Methylates the simple catechols guaiacol and
CC isovanillic acid as well as the tetrahydrobenzylisoquinolines (R)-
CC reticuline, (S)-reticuline, (R,S)-orientaline, (R)-protosinomenine and
CC (R,S)-isoorientaline. Involved in the production of laudanine.
CC {ECO:0000269|PubMed:14675446, ECO:0000269|PubMed:15353584,
CC ECO:0000269|PubMed:22725256, ECO:0000269|PubMed:23738019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-reticuline + S-adenosyl-L-methionine = (S)-laudanine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10444,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:57873,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:75999; EC=2.1.1.291;
CC Evidence={ECO:0000269|PubMed:14675446};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-reticuline + S-adenosyl-L-methionine = (R)-laudanine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38907,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58144,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:76001; EC=2.1.1.291;
CC Evidence={ECO:0000269|PubMed:14675446};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for guaiacol {ECO:0000269|PubMed:14675446};
CC KM=16 uM for (S)-reticuline {ECO:0000269|PubMed:14675446};
CC KM=17 uM for (R)-reticuline {ECO:0000269|PubMed:14675446};
CC KM=16 uM for (R)-protosinomenine {ECO:0000269|PubMed:14675446};
CC KM=17 uM for (R,S)-isoorientaline {ECO:0000269|PubMed:14675446};
CC KM=14 uM for isovanillic acid {ECO:0000269|PubMed:14675446};
CC KM=310 uM for S-adenosyl-L-methionine with guaiacol as substrate
CC {ECO:0000269|PubMed:14675446};
CC KM=360 uM for S-adenosyl-L-methionine with (S)-reticuline as
CC substrate {ECO:0000269|PubMed:14675446};
CC KM=310 uM for S-adenosyl-L-methionine with (R)-reticuline as
CC substrate {ECO:0000269|PubMed:14675446};
CC KM=320 uM for S-adenosyl-L-methionine with R)-protosinomenine as
CC substrate {ECO:0000269|PubMed:14675446};
CC KM=260 uM for S-adenosyl-L-methionine with (R,S)-isoorientaline as
CC substrate {ECO:0000269|PubMed:14675446};
CC KM=150 uM for S-adenosyl-L-methionine with isovanillic acid as
CC substrate {ECO:0000269|PubMed:14675446};
CC Note=kcat is 0.1 sec(-1) with guaiacol as substrate. kcat is 0.07
CC sec(-1) with (S)-reticuline as substrate. kcat is 0.07 sec(-1) with
CC (R)-reticuline as substrate. kcat is 0.03 sec(-1) with (R)-
CC protosinomenine as substrate. kcat is 0.02 sec(-1) with (R,S)-
CC isoorientaline as substrate. kcat is 0.02 sec(-1) with isovanillic
CC acid as substrate.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:14675446};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:14675446};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14675446}.
CC -!- TISSUE SPECIFICITY: Expressed in capsules, buds and stems, and at lower
CC levels in leaves. Localized to parenchyma cells within the vascular
CC bundle, but only to those cells distal to laticifers. In roots, found
CC in the pericycle within the stele. {ECO:0000269|PubMed:14675446,
CC ECO:0000269|PubMed:15353584}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY268893; AAQ01668.1; -; mRNA.
DR AlphaFoldDB; Q6WUC2; -.
DR SMR; Q6WUC2; -.
DR KEGG; ag:AAQ01668; -.
DR BRENDA; 2.1.1.291; 4515.
DR SABIO-RK; Q6WUC2; -.
DR GO; GO:0102918; F:(R)-reticuline 7-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102917; F:(S)-reticuline 7-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009821; P:alkaloid biosynthetic process; IDA:UniProtKB.
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 Alkaloid metabolism; Direct protein sequencing; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..355
FT /note="(R,S)-reticuline 7-O-methyltransferase"
FT /id="PRO_0000428642"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 197..200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 221..222
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 221
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 241..242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 355 AA; 39842 MW; DD408079B18D8F71 CRC64;
MDTAEERLKG QAEIWEHMFA FVDSMALKCA VELGIPDIIN SHGRPVTISE IVDSLKTNTP
SSSPNIDYLT RIMRLLVHKR LFTSELHQES NQLLYNLTRS SKWLLKDSKF NLSPLVLWET
NPILLKPWQY LGKCAQEKSS PFERAHGCEI WDLALADPKF NNFLNGAMQC STTTIINEML
LEYKDGFSGI AGSLVDVGGG TGSIIAEIVK AHPHIQGINF DLPHVVATAA EFPGVKHVGG
DMFVDIPEAD AVIMKWILHD WSDEDCTIIL KNCYRAIRKK KNGKVIIVDC VLRPDGNDLF
DKMGLIFDVL MMAHTTAGKE RTEAEWKILL NNAGFPRYNV IRTPAFPCII EAFPE
