ID   COOMT_COPJA             Reviewed;         351 AA.
AC   Q8H9A8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Columbamine O-methyltransferase;
DE            Short=CoOMT;
DE            EC=2.1.1.118;
DE   AltName: Full=Tetrahydrocolumbamine 2-O-methyltransferase;
DE            EC=2.1.1.89;
OS   Coptis japonica (Japanese goldthread).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Coptidoideae;
OC   Coptis.
OX   NCBI_TaxID=3442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12423366; DOI=10.1046/j.1432-1033.2002.03275.x;
RA   Morishige T., Dubouzet E., Choi K.-B., Yazaki K., Sato F.;
RT   "Molecular cloning of columbamine O-methyltransferase from cultured Coptis
RT   japonica cells.";
RL   Eur. J. Biochem. 269:5659-5667(2002).
CC   -!- FUNCTION: Catalyzes the conversion of tetrahydrocolumbamine to (S)-
CC       tetrahydropalmatine and of columbamine to palmatine, an isoquinoline
CC       alkaloid. {ECO:0000269|PubMed:12423366}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=columbamine + S-adenosyl-L-methionine = H(+) + palmatine + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:15373, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15920, ChEBI:CHEBI:16096, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789; EC=2.1.1.118;
CC         Evidence={ECO:0000269|PubMed:12423366};
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:12423366};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=66 uM for columbamine {ECO:0000269|PubMed:12423366};
CC         KM=35 uM for tetrahydrocolumbamine {ECO:0000269|PubMed:12423366};
CC         KM=173 uM for (S)-scoulerine {ECO:0000269|PubMed:12423366};
CC   -!- PATHWAY: Alkaloid biosynthesis; palmatine biosynthesis; palmatine from
CC       columbamine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AB073908; BAC22084.1; -; mRNA.
DR   AlphaFoldDB; Q8H9A8; -.
DR   SMR; Q8H9A8; -.
DR   KEGG; ag:BAC22084; -.
DR   BRENDA; 2.1.1.89; 1610.
DR   SABIO-RK; Q8H9A8; -.
DR   UniPathway; UPA00307; UER00445.
DR   GO; GO:0030778; F:columbamine 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:0030762; F:tetrahydrocolumbamine 2-O-methyltransferase activity; IEA:UniProtKB-EC.
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   Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..351
FT                   /note="Columbamine O-methyltransferase"
FT                   /id="PRO_0000204432"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         198
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
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         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   351 AA;  39282 MW;  B0D2B88F477F9A28 CRC64;
     MDTPNTFQND DEIKAQAQVW KHMFGFAETI MLRSTVSLGI PDIIHNNGPV TLSQLVTHLP
     LKSTSIDRFH HFMRYLVHMQ LFTISTDQIT KEDKYELTPA SKLLVHGHQK SLAPYVMLQT
     HPEEFSVWSH VINVLDGKKP YWESNDTSMY EKTEGDPEIN EILNDAMTSH STFMLPALVS
     GLMKENVLDG VASIVDVGGN SGVVAKGIVD AFPHVKCSVM DLNHVIERVI KNPKLDYVAG
     DMFTSIPNAD AILLKSTLHN YEDDDCIKIL NIAKEALPST GGKVILVEIV VDTENLPLFT
     SARLSMGMDM MLMSGKERTK KEWEDLLRKA NFTSHQVIPI MAIESIIVAY S