ID OMT2_CHRAE Reviewed; 343 AA. AC Q42653; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2009, entry version 50. DE RecName: Full=Quercetin 3-O-methyltransferase 2; DE EC=2.1.1.76; DE AltName: Full=Flavonol 3-O-methyltransferase 2; GN Name=OMT2; OS Chrysosplenium americanum (Golden saxifrage). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Saxifragales; Saxifragaceae; Chrysosplenium. OX NCBI_TaxID=36749; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RC TISSUE=Leaf; RX MEDLINE=98181116; PubMed=9514654; DOI=10.1006/abbi.1997.0554; RA Gauthier A., Gulick P.J., Ibrahim R.K.; RT "Characterization of two cDNA clones which encode O-methyltransferases RT for the methylation of both flavonoid and phenylpropanoid compounds."; RL Arch. Biochem. Biophys. 351:243-249(1998). CC -!- FUNCTION: Methylates OH residues of flavonoid and phenylpropanoid CC compounds and shows a higher affinity for flavonoid than CC phenylpropanoid substrates. Substrate preference is quercetin CC (flavonoid) = luteolin (flavonoid) = 5-hydroxyferulic acid CC (phenylpropanoid) > caffeic acid (phenylpropanoid) >> apigenin CC (flavonoid) = kempferol (flavonoid). 3,4-dimethylquercetin is not CC a substrate. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3,5,7,3',4'- CC pentahydroxyflavone = S-adenosyl-L-homocysteine + 3-methoxy- CC 5,7,3',4'-tetrahydroxyflavone. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Note=The Vmax value for flavonoid compounds methylation is two CC to threefold lower for OMT2 than for OMT1; CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type 2 CC family. COMT subfamily. CC -!- CAUTION: It is not sure if OMT1 and OMT2 are really encoded by two CC different genes or if they represent cloning artifacts. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U16793; AAA86982.1; -; mRNA. DR HSSP; P28002; 1KYZ. DR SMR; Q42653; 2-341. DR BRENDA; 2.1.1.76; 262661. DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0030755; F:quercetin 3-O-methyltransferase activity; IEA:EC. DR InterPro; IPR016461; O-MeTrfase_COMT_euk. DR InterPro; IPR001077; O_MeTrfase_2. DR InterPro; IPR012967; Plant_MeTrfase_dimerisation. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF08100; Dimerisation; 1. DR Pfam; PF00891; Methyltransf_2; 1. DR PIRSF; PIRSF005739; O-mtase; 1. PE 1: Evidence at protein level; KW Methyltransferase; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 343 Quercetin 3-O-methyltransferase 2. FT /FTId=PRO_0000063216. FT ACT_SITE 245 245 Proton acceptor (By similarity). FT BINDING 184 184 S-adenosyl-L-methionine; via carbonyl FT oxygen (By similarity). FT BINDING 207 207 S-adenosyl-L-methionine (By similarity). FT BINDING 227 227 S-adenosyl-L-methionine (By similarity). FT BINDING 228 228 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). FT BINDING 241 241 S-adenosyl-L-methionine (By similarity). SQ SEQUENCE 343 AA; 37868 MW; 8D363A98330FDE4F CRC64; MLFAMQLACA SVLPMVLKSA IELDLLEIIR GQDTCMSPTE IASHLPTTNP DAPAMVDRIL RLLSCYSVVT CSVRSVDDQR VYGLAPVCKY LTKNQDGVSI AALCLMNQDK VLMESWYHLK DAVLDGGIPF NKAYGMSSFE YHGTDPRFNK VFNRGMSDHS TITMKKVFQT YQGFQGLTSL VDVGGGTGAT LTMILSKYPT IRCINFDLPH VIEDAPEYPG IEHVGGDMFV SVPKGDAIFM KWICHDWSDE HCLKLLKNCY DALPNNGKVI LAECILPEVP DSSLATKGVV HIDVITVAHN PGGKERTEKE FEALAKAAGF QGFQVFCNAF NTYIIEFSKK ICN //