7OMT8_MEDSA
ID 7OMT8_MEDSA Reviewed; 352 AA.
AC O24529;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Isoflavone-7-O-methyltransferase 8;
DE EC=2.1.1.150;
DE AltName: Full=7-IOMT-8;
DE AltName: Full=Isoflavone-O-methyltransferase 8;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9484461; DOI=10.1023/a:1005938121453;
RA He X.-Z., Reddy J.T., Dixon R.A.;
RT "Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning and
RT characterization of an elicitor-inducible isoflavone 7-O-
RT methyltransferase.";
RL Plant Mol. Biol. 36:43-54(1998).
RN [2]
RP PROTEIN SEQUENCE OF 23-31; 77-105 AND 327-337, AND CHARACTERIZATION.
RX PubMed=8951042; DOI=10.1006/abbi.1996.0539;
RA He X.-Z., Dixon R.A.;
RT "Affinity chromatography, substrate/product specificity, and amino acid
RT sequence analysis of an isoflavone O-methyltransferase from alfalfa
RT (Medicago sativa L.).";
RL Arch. Biochem. Biophys. 336:121-129(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, AND
RP SUBUNIT.
RX PubMed=11224575; DOI=10.1038/85029;
RA Zubieta C., He X.-Z., Dixon R.A., Noel J.P.;
RT "Structures of two natural product methyltransferases reveal the basis for
RT substrate specificity in plant O-methyltransferases.";
RL Nat. Struct. Biol. 8:271-279(2001).
CC -!- FUNCTION: Transfers a methyl group to 7-hydroxyls of the isoflavones
CC daidzein, genistein and 6,7,4'-trihydroxyisoflavone. Can also methylate
CC (+)6a-hydroxymaackiain with lower efficiency.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 7-hydroxyisoflavone + S-adenosyl-L-methionine = a 7-
CC methoxyisoflavone + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:17933, ChEBI:CHEBI:15378, ChEBI:CHEBI:55465,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:140356;
CC EC=2.1.1.150;
CC -!- PATHWAY: Phytoalexin biosynthesis; medicarpin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11224575}.
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; U97125; AAC49928.1; -; mRNA.
DR PIR; T09707; T09707.
DR PDB; 1FP2; X-ray; 1.40 A; A=1-352.
DR PDB; 6CIG; X-ray; 1.65 A; A=1-352.
DR PDBsum; 1FP2; -.
DR PDBsum; 6CIG; -.
DR AlphaFoldDB; O24529; -.
DR SMR; O24529; -.
DR KEGG; ag:AAC49928; -.
DR BRENDA; 2.1.1.150; 3078.
DR BRENDA; 2.1.1.270; 3078.
DR UniPathway; UPA00902; -.
DR EvolutionaryTrace; O24529; -.
DR GO; GO:0033800; F:isoflavone 7-O-methyltransferase activity; IEA:UniProtKB-EC.
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 3D-structure; Direct protein sequencing; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..352
FT /note="Isoflavone-7-O-methyltransferase 8"
FT /id="PRO_0000204437"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT BINDING 118..127
FT /ligand="substrate"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 83..96
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1FP2"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1FP2"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:1FP2"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:1FP2"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:1FP2"
SQ SEQUENCE 352 AA; 39604 MW; 31B95228986C1296 CRC64;
MASSINGRKP SEIFKAQALL YKHIYAFIDS MSLKWAVEMN IPNIIQNHGK PISLSNLVSI
LQVPSSKIGN VRRLMRYLAH NGFFEIITKE EESYALTVAS ELLVRGSDLC LAPMVECVLD
PTLSGSYHEL KKWIYEEDLT LFGVTLGSGF WDFLDKNPEY NTSFNDAMAS DSKLINLALR
DCDFVFDGLE SIVDVGGGTG TTAKIICETF PKLKCIVFDR PQVVENLSGS NNLTYVGGDM
FTSIPNADAV LLKYILHNWT DKDCLRILKK CKEAVTNDGK RGKVTIIDMV IDKKKDENQV
TQIKLLMDVN MACLNGKERN EEEWKKLFIE AGFQHYKISP LTGFLSLIEI YP
