ID   OMT3_HUMLU              Reviewed;         377 AA.
AC   B0ZB57;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable O-methyltransferase 3 {ECO:0000303|PubMed:18223037};
DE            Short=HlOMT3 {ECO:0000303|PubMed:18223037};
DE            EC=2.1.1.- {ECO:0000305};
GN   Name=OMT3 {ECO:0000303|PubMed:18223037};
OS   Humulus lupulus (European hop).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Humulus.
OX   NCBI_TaxID=3486 {ECO:0000312|EMBL:ABZ89567.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Lupulin gland;
RX   PubMed=18223037; DOI=10.1105/tpc.107.055178;
RA   Nagel J., Culley L.K., Lu Y., Liu E., Matthews P.D., Stevens J.F.,
RA   Page J.E.;
RT   "EST analysis of hop glandular trichomes identifies an O-methyltransferase
RT   that catalyzes the biosynthesis of xanthohumol.";
RL   Plant Cell 20:186-200(2008).
CC   -!- TISSUE SPECIFICITY: Highly expressed in lupulin glands. Detected in
CC       early-, mid- and late-stage cones. {ECO:0000269|PubMed:18223037}.
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; EU309727; ABZ89567.1; -; mRNA.
DR   AlphaFoldDB; B0ZB57; -.
DR   SMR; B0ZB57; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..377
FT                   /note="Probable O-methyltransferase 3"
FT                   /id="PRO_0000439266"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
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"
SQ   SEQUENCE   377 AA;  42128 MW;  CEF1565C855019BA CRC64;
     MEKLKSFRHL NNNIDLILNE ENSTEILGAQ AHIWNQIFNF INSMSLKCAI QLGIPDIINN
     HGKPMTISQL TLALPINRKK SPCVYRLMRI LIHSGFFALQ KAEVGEEGGG EEEGYVITDA
     SKLLLKDNPM SVTPFLLAML DPVMTKPWDF LSNWFQNGDP TPFDTANGMA FWDYGSHEPK
     LARFFNDAMA SDARLVTSVV IEKCKGVFEG VESLVDVGGG TGTVASSIAA AFPHIQCTVF
     DLPHVVADLQ GGNNLNFVGG DMFVDVPATE VVLLKWILHD WNDEESVKIL KKCKEAISKS
     NKKGGKVIII DMKVENEKDE DDESYETQLF FDMLMMALVT GRERNEKEWA KLFKDAGFSN
     YKITPILGLR SLIEVYP