ID   OMT2_SORBI              Reviewed;         372 AA.
AC   A8QW51;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable O-methyltransferase 2;
DE            Short=SbOMT2;
DE            EC=2.1.1.-;
GN   Name=OMT2; OrderedLocusNames=Sb05g027340;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. BTx623;
RX   PubMed=17998204; DOI=10.1074/jbc.m706587200;
RA   Baerson S.R., Dayan F.E., Rimando A.M., Nanayakkara N.P., Liu C.J.,
RA   Schroder J., Fishbein M., Pan Z., Kagan I.A., Pratt L.H.,
RA   Cordonnier-Pratt M.M., Duke S.O.;
RT   "A functional genomics investigation of allelochemical biosynthesis in
RT   Sorghum bicolor root hairs.";
RL   J. Biol. Chem. 283:3231-3247(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623;
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA   Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
CC   -!- FUNCTION: O-methyltransferase of unknown substrate specificity. Not
CC       active on resorcinol, orcinol, guaiacol, eugenol, ferulic acid, p-
CC       coumaric acid, catechol, caffeic acid or monomethyl ethers of
CC       resorcinol or orcinol.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in root hairs.
CC       {ECO:0000269|PubMed:17998204}.
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; EF189706; ABP01562.1; -; mRNA.
DR   EMBL; CM000764; EES09025.1; -; Genomic_DNA.
DR   RefSeq; XP_002450037.1; XM_002449992.1.
DR   AlphaFoldDB; A8QW51; -.
DR   SMR; A8QW51; -.
DR   STRING; 4558.Sb05g027340.1; -.
DR   EnsemblPlants; EES09025; EES09025; SORBI_3005G224400.
DR   Gramene; EES09025; EES09025; SORBI_3005G224400.
DR   eggNOG; KOG3178; Eukaryota.
DR   HOGENOM; CLU_005533_7_0_1; -.
DR   InParanoid; A8QW51; -.
DR   OMA; GTVIREC; -.
DR   Proteomes; UP000000768; Chromosome 5.
DR   GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IBA:GO_Central.
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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..372
FT                   /note="Probable O-methyltransferase 2"
FT                   /id="PRO_0000409378"
FT   ACT_SITE        277
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   372 AA;  40898 MW;  82A4997A79F72983 CRC64;
     MAASSHAIAP TDAELLQAQA DLWRHSLYYL TSMALKCAVE LHIPTAIHNL GGATTLPDLV
     TALSLPKTKL PFLGRIMRLL VTSGIFASDG ANGDGAAAEA VYRLNPLSWL LVEGVESEDH
     TYQKYFVLAT VSQHYVDAGL SLADWFRKDL PEPLPSPFEC LHGVPLAHES TKLLDEELDR
     IVEEGVAAHD NLAIGTIIRE CSDIFSGLHS LTYCCGRQGN ISATAIIKAF PDIKCTVLNL
     PRVIETAPAD DAVSSVTGDL FHTIPPAQAV MLKLVLHFWS DEDCVKILEQ CRKAIPSREE
     GGKVIIIEIL LGPYMGPIMY EAQLLMDMLM MVNTRGRQRT ENDWRQIFTK AGFSDYKIVK
     KIGARGVIEV YP