OMT1_SORBI
ID OMT1_SORBI Reviewed; 376 AA.
AC A8QW52; C5YHU3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Eugenol O-methyltransferase;
DE EC=2.1.1.146;
DE AltName: Full=O-methyltransferase 1;
DE Short=SbOMT1;
GN Name=EOMT; Synonyms=OMT1; OrderedLocusNames=Sb07g004660;
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], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP 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. Substrate preference is eugenol >>
CC orcinol monomethyl ether > resorcinol monomethyl ether.
CC {ECO:0000269|PubMed:17998204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + trans-isoeugenol = H(+) + S-
CC adenosyl-L-homocysteine + trans-isomethyleugenol;
CC Xref=Rhea:RHEA:17081, ChEBI:CHEBI:6877, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:50545, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.146; Evidence={ECO:0000269|PubMed:17998204};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EES14631.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF189707; ABP01563.1; -; mRNA.
DR EMBL; CM000766; EES14631.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002445136.1; XM_002445091.1.
DR AlphaFoldDB; A8QW52; -.
DR SMR; A8QW52; -.
DR STRING; 4558.Sb07g004660.1; -.
DR EnsemblPlants; KXG24554; KXG24554; SORBI_3007G058400.
DR GeneID; 8080888; -.
DR Gramene; KXG24554; KXG24554; SORBI_3007G058400.
DR KEGG; sbi:8080888; -.
DR eggNOG; KOG3178; Eukaryota.
DR InParanoid; A8QW52; -.
DR OMA; SGFTNCK; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000000768; Chromosome 7.
DR ExpressionAtlas; A8QW52; baseline and differential.
DR GO; GO:0050630; F:(iso)eugenol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0102719; F:S-adenosyl-L-methionine:eugenol-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
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 Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..376
FT /note="Eugenol O-methyltransferase"
FT /id="PRO_0000409377"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 219
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 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 276
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 376 AA; 40847 MW; 67393CA7361E97AA CRC64;
MASYTSTSGQ FAVGKVAAAN QDDETCMHAL KLLGGLAVPF TIKAVIELGI MDLLLAADRA
MTAEALTAAL LCPAPAPAAA AAMVDRMLRF LASHGVVRCA TESEELGSDD GKSCRRYAAA
PVCKWFARGG GVESVVPMGF WMTSTTNMET WHNIKDGVLA GETPFDKAYG MPVFEYLGAN
GTMNTLFNEA MASHSMIITK RLLEVFRGFE NYSVLVDVGG GNGTTMQMIR SQYENISGIN
YDLPHVIAQA SPIEGVEHVA GNMFDNIPRG DAIILKWILH NWGDKECVKI LKNCYTALPV
NGTVIILEYI LPETPEETLA SQLAFDFDLG MMLFFGASGK ERTEKELLEL AREAGFSGDY
TATYIFANVW AHEFTK
