6OMT_THLFG
ID 6OMT_THLFG Reviewed; 350 AA.
AC Q5C9L7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=(RS)-norcoclaurine 6-O-methyltransferase {ECO:0000303|PubMed:27232113};
DE EC=2.1.1.128 {ECO:0000269|PubMed:27232113};
OS Thalictrum flavum subsp. glaucum (Yellow meadow rue).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Thalictrum.
OX NCBI_TaxID=150095;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15722473; DOI=10.1105/tpc.104.028654;
RA Samanani N., Park S.U., Facchini P.J.;
RT "Cell type-specific localization of transcripts encoding nine consecutive
RT enzymes involved in protoberberine alkaloid biosynthesis.";
RL Plant Cell 17:915-926(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 3-350 IN COMPLEX WITH SUBSTRATE
RP ANALOG AND S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND HOMODIMERIZATION.
RX PubMed=27232113; DOI=10.1111/tpj.13225;
RA Robin A.Y., Giustini C., Graindorge M., Matringe M., Dumas R.;
RT "Crystal structure of norcoclaurine-6-O-methyltransferase, a key rate-
RT limiting step in the synthesis of benzylisoquinoline alkaloids.";
RL Plant J. 87:641-653(2016).
CC -!- FUNCTION: Involved in the biosynthesis of coclaurine, a precursor of
CC benzylisoquinoline alkaloids (PubMed:27232113). Catalyzes the transfer
CC of the S-methyl group of S-adenosyl-L-methionine (AdoMet) to the 6-
CC hydroxyl group of norcoclaurine to form coclaurine (PubMed:27232113).
CC {ECO:0000269|PubMed:27232113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-norcoclaurine + S-adenosyl-L-methionine = (S)-coclaurine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31907,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57581, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58253, ChEBI:CHEBI:59789; EC=2.1.1.128;
CC Evidence={ECO:0000269|PubMed:27232113};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=norcoclaurine + S-adenosyl-L-methionine = coclaurine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19941, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58481, ChEBI:CHEBI:58482,
CC ChEBI:CHEBI:59789; EC=2.1.1.128;
CC Evidence={ECO:0000269|PubMed:27232113};
CC -!- ACTIVITY REGULATION: Inhibited by sanguinarine.
CC {ECO:0000269|PubMed:27232113}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for norcoclaurine {ECO:0000269|PubMed:27232113};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27232113}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf primordia of rhizomes and root
CC endodermis. {ECO:0000269|PubMed:15722473}.
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; AY610507; AAU20765.1; -; mRNA.
DR PDB; 5ICC; X-ray; 1.90 A; A=3-350.
DR PDB; 5ICE; X-ray; 1.60 A; A=3-350.
DR PDB; 5ICF; X-ray; 1.80 A; A=3-350.
DR PDB; 5ICG; X-ray; 2.60 A; A=8-350.
DR PDBsum; 5ICC; -.
DR PDBsum; 5ICE; -.
DR PDBsum; 5ICF; -.
DR PDBsum; 5ICG; -.
DR AlphaFoldDB; Q5C9L7; -.
DR SMR; Q5C9L7; -.
DR GO; GO:0030786; F:(RS)-norcoclaurine 6-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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..350
FT /note="(RS)-norcoclaurine 6-O-methyltransferase"
FT /id="PRO_0000446976"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICC, ECO:0007744|PDB:5ICE,
FT ECO:0007744|PDB:5ICF"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICE"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICC, ECO:0007744|PDB:5ICE,
FT ECO:0007744|PDB:5ICF"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICC, ECO:0007744|PDB:5ICE,
FT ECO:0007744|PDB:5ICF"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020,
FT ECO:0000269|PubMed:27232113, ECO:0007744|PDB:5ICC,
FT ECO:0007744|PDB:5ICE, ECO:0007744|PDB:5ICF"
FT BINDING 238..239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICC, ECO:0007744|PDB:5ICE,
FT ECO:0007744|PDB:5ICF"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICC, ECO:0007744|PDB:5ICE,
FT ECO:0007744|PDB:5ICF"
FT BINDING 253..257
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICE"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27232113,
FT ECO:0007744|PDB:5ICE"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:5ICE"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:5ICE"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:5ICE"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:5ICE"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:5ICE"
SQ SEQUENCE 350 AA; 39385 MW; D73A25638E89CC77 CRC64;
MEMINKENLS SQAKLWNFIY GFADSLVLKS AVQLDLANII HNHGSPMTLS ELSLHLPSQP
VNQDALYRVL RYLVHMKLFT KSSIDGELRY GLAPPAKFLV KGWDKCMLGA ILTITDKDFM
APWHYLKEGI LNDGSTSTAF EKALGTNIWD YMAEHPEKNQ LFNEGMANDT RLIMSALVKE
CSSMFDGITT IVDVGGGTGT AVRNIAKAFP HIKCTVYDLP HVIADSPGYT EINSIQGDMF
KYIPNADAIM MKCILHDWDD KECIEILKRC KDAVPRDGGK VIIIDIILDV KSEHPYTKMR
LTLDLDMMLN TGGKERTEEE WKKLIHDAGY KGYKITHISA VQSVIEAYPY
