OMT3_SORBI
ID OMT3_SORBI Reviewed; 374 AA.
AC A8QW53;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=5-pentadecatrienyl resorcinol O-methyltransferase;
DE EC=2.1.1.n7;
DE AltName: Full=O-methyltransferase 3;
DE Short=SbOMT3;
GN Name=OMT3; OrderedLocusNames=Sb06g000820;
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, 3D-STRUCTURE MODELING, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 involved in the biosynthetic pathway of
CC the phytotoxin sorgoleone, a potent broad-spectrum inhibitor active
CC against many agronomically important monocot and dicot weed species.
CC Substrate specificity for alkylresorcinols. Strong preference for a
CC five carbons alkyl side chain. {ECO:0000269|PubMed:17998204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z)-5-(pentadeca-8,11,14-trien-1-yl)resorcinol + S-
CC adenosyl-L-methionine = (8Z,11Z)-5-(pentadeca- 8,11,14-trien-1-
CC yl)resorcinol-3-methyl ether + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:26325, ChEBI:CHEBI:15378, ChEBI:CHEBI:52680,
CC ChEBI:CHEBI:52681, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.n7;
CC Evidence={ECO:0000269|PubMed:17998204};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1436 uM for 5-n-propyl-resorcinol {ECO:0000269|PubMed:17998204};
CC KM=481 uM for 5-n-butyl-resorcinol {ECO:0000269|PubMed:17998204};
CC KM=152 uM for 5-n-pentyl-resorcinol {ECO:0000269|PubMed:17998204};
CC KM=72 uM for 5-n-hexyl-resorcinol {ECO:0000269|PubMed:17998204};
CC KM=23 uM for 5-n-heptyl-resorcinol {ECO:0000269|PubMed:17998204};
CC KM=67.5 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:17998204};
CC Vmax=4.3 pmol/sec/mg enzyme with 5-n-propyl-resorcinol as methyl
CC acceptor {ECO:0000269|PubMed:17998204};
CC Vmax=9.2 pmol/sec/mg enzyme with 5-n-butyl-resorcinol as methyl
CC acceptor {ECO:0000269|PubMed:17998204};
CC Vmax=10.9 pmol/sec/mg enzyme with 5-n-pentyl-resorcinol as methyl
CC acceptor {ECO:0000269|PubMed:17998204};
CC Vmax=7.0 pmol/sec/mg enzyme with 5-n-hexyl-resorcinol as methyl
CC acceptor {ECO:0000269|PubMed:17998204};
CC Vmax=2.9 pmol/sec/mg enzyme with 5-n-heptyl-resorcinol as methyl
CC acceptor {ECO:0000269|PubMed:17998204};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; EF189708; ABP01564.1; -; mRNA.
DR EMBL; CM000765; EES11753.1; -; Genomic_DNA.
DR RefSeq; XP_002447425.1; XM_002447380.1.
DR AlphaFoldDB; A8QW53; -.
DR SMR; A8QW53; -.
DR STRING; 4558.Sb06g000820.1; -.
DR EnsemblPlants; EES11753; EES11753; SORBI_3006G007900.
DR GeneID; 8080259; -.
DR Gramene; EES11753; EES11753; SORBI_3006G007900.
DR KEGG; sbi:8080259; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_7_0_1; -.
DR InParanoid; A8QW53; -.
DR OMA; HMINAES; -.
DR OrthoDB; 817726at2759; -.
DR BRENDA; 2.1.1.240; 5768.
DR Proteomes; UP000000768; Chromosome 6.
DR GO; GO:0102990; F:5-n-alk(en)ylresorcinol O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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..374
FT /note="5-pentadecatrienyl resorcinol O-methyltransferase"
FT /id="PRO_0000409379"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 374 AA; 40884 MW; B7EEABE89D15D844 CRC64;
MVLISEDSRE LLQAHVELWN QTYSFMKSVA LAVALDLHIA DAIHRRGGAA TLSQILGEIG
VRPCKLPGLH RIMRVLTVSG TFTIVQPSAE TMSSESDGRE PVYKLTTASS LLVSSESSAT
ASLSPMLNHV LSPFRDSPLS MGLTAWFRHD EDEQAPGMCP FTLMYGTTLW EVCRRDDAIN
ALFNNAMAAD SNFLMQILLK EFSEVFLGID SLVDVAGGVG GATMAIAAAF PCLKCTVLDL
PHVVAKAPSS SIGNVQFVGG DMFESIPPAN VVLLKWILHD WSNDECIKIL KNCKQAIPSR
DAGGKIIIID VVVGSDSSDT KLLETQVIYD LHLMKIGGVE RDEQEWKKIF LEAGFKDYKI
MPILGLRSII ELYP
