OMT1_HUMLU
ID OMT1_HUMLU Reviewed; 352 AA.
AC B0ZB55; B6EFA6;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Desmethylxanthohumol 6'-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.338 {ECO:0000269|PubMed:18223037};
DE AltName: Full=O-methyltransferase 1 {ECO:0000303|PubMed:18223037};
DE Short=HlOMT1 {ECO:0000303|PubMed:18223037};
GN Name=OMT1 {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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, SUBSTRATE SPECIFICITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=cv. Taurus; 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Osvald's 72; TISSUE=Female cone, and Lupulin gland;
RA Matousek J., Patzak J., Kocabek T., Fussy Z., Heyerick A., Krofta K.;
RT "Cloning of variant of OMT1 from Czech hop Osvald's 72 and analysis of
RT metabolome changes upon its expression in heterologous plant
RT transgenotes.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=29760092; DOI=10.1073/pnas.1802223115;
RA Ban Z., Qin H., Mitchell A.J., Liu B., Zhang F., Weng J.-K., Dixon R.A.,
RA Wang G.;
RT "Noncatalytic chalcone isomerase-fold proteins in Humulus lupulus are
RT auxiliary components in prenylated flavonoid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E5223-E5232(2018).
RN [4]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of prenylated phenolics natural
CC products which contribute to the bitter taste of beer and display broad
CC biological activities (Probable). Catalyzes the biosynthesis of
CC xanthohumol (PubMed:18223037). Methylates desmethylxanthohumol and
CC xanthogalenol, but not caffeic acid, prenylflavanones, simple phenols
CC or phenylpropanoids (PubMed:18223037). {ECO:0000269|PubMed:18223037,
CC ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=desmethylxanthohumol + S-adenosyl-L-methionine = H(+) + S-
CC adenosyl-L-homocysteine + xanthohumol; Xref=Rhea:RHEA:51696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134289, ChEBI:CHEBI:134302; EC=2.1.1.338;
CC Evidence={ECO:0000269|PubMed:18223037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51697;
CC Evidence={ECO:0000269|PubMed:18223037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + xanthogalenol = 4'-O-
CC methylxanthohumol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:134308, ChEBI:CHEBI:134309;
CC EC=2.1.1.338; Evidence={ECO:0000269|PubMed:18223037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51701;
CC Evidence={ECO:0000269|PubMed:18223037};
CC -!- ACTIVITY REGULATION: Inhibited by S-adenosyl homocysteine.
CC {ECO:0000269|PubMed:18223037}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for desmethylxanthohumol {ECO:0000269|PubMed:18223037};
CC KM=286 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18223037};
CC Vmax=55 pmol/sec/mg enzyme toward desmethylxanthohumol
CC {ECO:0000269|PubMed:18223037};
CC Vmax=56 pmol/sec/mg enzyme toward S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:18223037};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:18223037};
CC Temperature dependence:
CC Optimum temperature is 30-37 degrees Celsius.;
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18223037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29760092}.
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; EU309725; ABZ89565.1; -; mRNA.
DR EMBL; FM164641; CAQ58423.1; -; mRNA.
DR AlphaFoldDB; B0ZB55; -.
DR SMR; B0ZB55; -.
DR KEGG; ag:ABZ89565; -.
DR BRENDA; 2.1.1.338; 2716.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..352
FT /note="Desmethylxanthohumol 6'-O-methyltransferase"
FT /id="PRO_0000439264"
FT ACT_SITE 257
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 CONFLICT 157
FT /note="D -> E (in Ref. 2; CAQ58423)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> M (in Ref. 2; CAQ58423)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="S -> C (in Ref. 2; CAQ58423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39266 MW; C36351EE8FA13976 CRC64;
MESLRGQEQI WQLMFSFVDS MALKCAIELR IADIIHSHGK PITLSQIASG IRSNSNSSIS
PNIPYLSRIM RFLVRKNIFT EHQEDNDEVI SLYGLSDSSR WLLRDFKSSL APMVLMQTHP
LSMAVWHFLE DYVRNSSNTF EKAHGCNIWE FSSANPDFNK IFNNAMASIV PIYMGAVLSS
YKDGLGCIKG TVVDVGGGTG GSISELMKYY PNIKGINFDL PHVIATAPAL DGVTHISGDI
FESIPSADAV LMKGVLHCFS DEKCVKVLRN CRKAITDKKN GKIIILEIVL DPTSNQIFDE
TRMVYDLLIP LFSGGKERTE LEWKRLLNEA GFTSIKITKI PIIPAIIEAF LV
