SOMT1_PAPSO
ID SOMT1_PAPSO Reviewed; 390 AA.
AC I3V6A7; I3PLQ5;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Scoulerine-9-O-methyltransferase 1 {ECO:0000303|PubMed:22535422};
DE Short=PsSOMT1 {ECO:0000303|PubMed:22535422};
DE EC=2.1.1.117 {ECO:0000269|PubMed:22535422, ECO:0000269|PubMed:22653730, ECO:0000269|Ref.5};
DE AltName: Full=Norreticuline 3-O-methyltransferase SOMT1 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:22535422};
DE AltName: Full=O-methyltransferase 1 {ECO:0000303|PubMed:22653730};
DE AltName: Full=Reticuline 3-O-methyltransferase SOMT1 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:22535422};
DE AltName: Full=Tetrahydrocolumbamine 2-O-methyltransferase SOMT1 {ECO:0000305};
DE EC=2.1.1.89 {ECO:0000269|PubMed:22535422};
GN Name=SOMT1 {ECO:0000303|PubMed:22535422};
GN Synonyms=PSMT1 {ECO:0000303|PubMed:22653730};
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].
RX PubMed=22527754; DOI=10.1007/s11103-012-9913-2;
RA Desgagne-Penix I., Farrow S.C., Cram D., Nowak J., Facchini P.J.;
RT "Integration of deep transcript and targeted metabolite profiles for eight
RT cultivars of opium poppy.";
RL Plant Mol. Biol. 79:295-313(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=22653730; DOI=10.1126/science.1220757;
RA Winzer T., Gazda V., He Z., Kaminski F., Kern M., Larson T.R., Li Y.,
RA Meade F., Teodor R., Vaistij F.E., Walker C., Bowser T.A., Graham I.A.;
RT "A Papaver somniferum 10-gene cluster for synthesis of the anticancer
RT alkaloid noscapine.";
RL Science 336:1704-1708(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=22535422; DOI=10.1104/pp.112.194886;
RA Dang T.T., Facchini P.J.;
RT "Characterization of three O-methyltransferases involved in noscapine
RT biosynthesis in opium poppy.";
RL Plant Physiol. 159:618-631(2012).
RN [4]
RP FUNCTION.
RX PubMed=29610307; DOI=10.1073/pnas.1721469115;
RA Li Y., Li S., Thodey K., Trenchard I., Cravens A., Smolke C.D.;
RT "Complete biosynthesis of noscapine and halogenated alkaloids in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E3922-E3931(2018).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, AND
RP MUTAGENESIS OF HIS-296.
RX DOI=10.1021/acscatal.9b01038;
RA Cabry M.P., Offen W.A., Saleh P., Li Y., Winzer T., Graham I.A.,
RA Davies G.J.;
RT "Structure of Papaver somniferum O-methyltransferase 1 reveals initiation
RT of noscapine biosynthesis with implications for plant natural product
RT methylation.";
RL ACS Catal. 9:3840-3848(2019).
CC -!- FUNCTION: Methyltransferase involved in the biosynthesis of the
CC benzylisoquinoline alkaloid noscapine (PubMed:22535422,
CC PubMed:22653730, PubMed:29610307). Catalyzes the conversion of (S)-
CC scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422,
CC PubMed:22653730). Can convert (S)-tetrahydrocolumbamine to
CC tetrahydropalmatine (PubMed:22535422). Can convert (S)-norreticuline to
CC (S)-norcodamine (PubMed:22535422). Can convert (S)-reticuline to (S)-
CC codamine (PubMed:22535422). Substrate preference is (S)-scoulerine >
CC (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline
CC (PubMed:22535422). {ECO:0000269|PubMed:22535422,
CC ECO:0000269|PubMed:22653730, ECO:0000269|PubMed:29610307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-scoulerine + S-adenosyl-L-methionine = (S)-
CC tetrahydrocolumbamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:23808, ChEBI:CHEBI:15378, ChEBI:CHEBI:17129,
CC ChEBI:CHEBI:17772, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.117; Evidence={ECO:0000269|PubMed:22535422,
CC ECO:0000269|PubMed:22653730, ECO:0000269|Ref.5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23809;
CC Evidence={ECO:0000305|PubMed:22535422};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-tetrahydrocolumbamine + S-adenosyl-L-methionine = H(+) +
CC S-adenosyl-L-homocysteine + tetrahydropalmatine;
CC Xref=Rhea:RHEA:22536, ChEBI:CHEBI:15378, ChEBI:CHEBI:16563,
CC ChEBI:CHEBI:17772, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.89;
CC Evidence={ECO:0000269|PubMed:22535422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22537;
CC Evidence={ECO:0000305|PubMed:22535422};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-norreticuline + S-adenosyl-L-methionine = (S)-norcodamine
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:22180,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:143271, ChEBI:CHEBI:143273;
CC Evidence={ECO:0000269|PubMed:22535422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22181;
CC Evidence={ECO:0000305|PubMed:22535422};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-reticuline + S-adenosyl-L-methionine = (S)-codamine + H(+)
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:59532, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:57873, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:143148; Evidence={ECO:0000269|PubMed:22535422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59533;
CC Evidence={ECO:0000305|PubMed:22535422};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28.5 uM for (S)-scoulerine {ECO:0000269|PubMed:22535422};
CC KM=70.3 uM for (S)-reticuline {ECO:0000269|PubMed:22535422};
CC KM=19 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:22535422};
CC Vmax=2036 nmol/min/mg enzyme with (S)-scoulerine as substrate
CC {ECO:0000269|PubMed:22535422};
CC Vmax=184.4 nmol/min/mg enzyme with (S)-reticuline as substrate
CC {ECO:0000269|PubMed:22535422};
CC Vmax=1290 nmol/min/mg enzyme with S-adenosyl-L-methionine as
CC substrate {ECO:0000269|PubMed:22535422};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.5}.
CC -!- TISSUE SPECIFICITY: Highly expressed in capsules (PubMed:22653730).
CC Expressed is stems (PubMed:22653730, PubMed:22535422). Expressed at low
CC levels in roots (PubMed:22535422). {ECO:0000269|PubMed:22535422,
CC ECO:0000269|PubMed:22653730}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; JN185323; AFK73709.1; -; mRNA.
DR EMBL; JQ658999; AFB74611.1; -; Genomic_DNA.
DR PDB; 6I5Q; X-ray; 3.05 A; A/B/C/D=1-390.
DR PDB; 6I5Z; X-ray; 3.00 A; A/B/C/D=1-390.
DR PDB; 6I6K; X-ray; 1.49 A; A/B=1-390.
DR PDB; 6I6L; X-ray; 1.29 A; A/B=1-390.
DR PDB; 6I6M; X-ray; 1.20 A; A/B=1-390.
DR PDB; 6I6N; X-ray; 1.50 A; A/B=1-390.
DR PDBsum; 6I5Q; -.
DR PDBsum; 6I5Z; -.
DR PDBsum; 6I6K; -.
DR PDBsum; 6I6L; -.
DR PDBsum; 6I6M; -.
DR PDBsum; 6I6N; -.
DR AlphaFoldDB; I3V6A7; -.
DR SMR; I3V6A7; -.
DR GO; GO:0030777; F:(S)-scoulerine 9-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0030762; F:tetrahydrocolumbamine 2-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009708; P:benzyl isoquinoline 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 3D-structure; Alkaloid metabolism; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..390
FT /note="Scoulerine-9-O-methyltransferase 1"
FT /id="PRO_0000447591"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000269|Ref.5"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:6I6K, ECO:0007744|PDB:6I6N"
FT BINDING 207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5C9L7"
FT BINDING 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:6I6K,
FT ECO:0007744|PDB:6I6N"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:6I6K,
FT ECO:0007744|PDB:6I6N"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:6I6K,
FT ECO:0007744|PDB:6I6N"
FT BINDING 278..279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:6I6K,
FT ECO:0007744|PDB:6I6N"
FT BINDING 292
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:6I6K,
FT ECO:0007744|PDB:6I6N"
FT BINDING 296..297
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:6I6K,
FT ECO:0007744|PDB:6I6N"
FT MUTAGEN 296
FT /note="H->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|Ref.5"
FT CONFLICT 15..17
FT /note="RQT -> HQS (in Ref. 2; AFB74611)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="F -> V (in Ref. 2; AFB74611)"
FT /evidence="ECO:0000305"
FT HELIX 35..57
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6I6N"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:6I6M"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 197..221
FT /evidence="ECO:0007829|PDB:6I6M"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6I6M"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6I5Z"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6I6M"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:6I6M"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:6I6M"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:6I6M"
SQ SEQUENCE 390 AA; 42699 MW; C3E59F1D7F78BE01 CRC64;
MATNGEIFNT YGHNRQTATV TKITASNESS NGVCYLSETA NLGKLICIPM ALRAAMELNV
FQLISKFGTD AKVSASEIAS KMPNAKNNPE AAMYLDRILR LLGASSILSV STTKKSINRG
GDDVVVHEKL YGLTNSSCCL VPRQEDGVSL VEELLFTSDK VVVDSFFKLK CVVEEKDSVP
FEVAHGAKIF EYAATEPRMN QVFNDGMAVF SIVVFEAVFR FYDGFLDMKE LLDVGGGIGT
SVSKIVAKYP LIRGVNFDLP HVISVAPQYP GVEHVAGDMF EEVPKGQNML LKWVLHDWGD
ERCVKLLKNC WNSLPVGGKV LIIEFVLPNE LGNNAESFNA LIPDLLLMAL NPGGKERTIS
EYDDLGKAAG FIKTIPIPIS NGLHVIEFHK
