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Protein

Isoflavone-7-O-methyltransferase 8

Gene
N/A
Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transfers a methyl group to 7-hydroxyls of the isoflavones daidzein, genistein and 6,7,4'-trihydroxyisoflavone. Can also methylate (+)6a-hydroxymaackiain with lower efficiency.

Catalytic activityi

S-adenosyl-L-methionine + a 7-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 7-methoxyisoflavone.

Pathwayi: medicarpin biosynthesis

This protein is involved in the pathway medicarpin biosynthesis, which is part of Phytoalexin biosynthesis.
View all proteins of this organism that are known to be involved in the pathway medicarpin biosynthesis and in Phytoalexin biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei196 – 1961S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei219 – 2191S-adenosyl-L-methionine
Binding sitei239 – 2391S-adenosyl-L-methionine
Binding sitei240 – 2401S-adenosyl-L-methionine; via amide nitrogen
Binding sitei253 – 2531S-adenosyl-L-methionine
Active sitei257 – 2571Proton acceptor

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.150. 3078.
2.1.1.270. 3078.
UniPathwayiUPA00902.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoflavone-7-O-methyltransferase 8 (EC:2.1.1.150)
Alternative name(s):
7-IOMT-8
Isoflavone-O-methyltransferase 8
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Isoflavone-7-O-methyltransferase 8PRO_0000204437Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 2413Combined sources
Helixi27 – 3812Combined sources
Helixi41 – 488Combined sources
Helixi54 – 618Combined sources
Helixi65 – 673Combined sources
Helixi68 – 8013Combined sources
Beta strandi83 – 9614Combined sources
Helixi98 – 1014Combined sources
Beta strandi107 – 1093Combined sources
Helixi112 – 1187Combined sources
Helixi121 – 1255Combined sources
Helixi126 – 1294Combined sources
Helixi130 – 1345Combined sources
Helixi141 – 1466Combined sources
Helixi150 – 1567Combined sources
Helixi158 – 17013Combined sources
Helixi172 – 1809Combined sources
Helixi183 – 1864Combined sources
Beta strandi190 – 1956Combined sources
Helixi201 – 2099Combined sources
Beta strandi214 – 2196Combined sources
Helixi221 – 2244Combined sources
Beta strandi233 – 2375Combined sources
Turni240 – 2423Combined sources
Beta strandi248 – 2547Combined sources
Helixi256 – 2583Combined sources
Helixi261 – 27515Combined sources
Helixi277 – 2793Combined sources
Beta strandi283 – 2886Combined sources
Turni293 – 2953Combined sources
Helixi298 – 31013Combined sources
Helixi311 – 3144Combined sources
Helixi321 – 33010Combined sources
Beta strandi335 – 3428Combined sources
Beta strandi345 – 3517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FP2X-ray1.40A1-352[»]
1FPXX-ray1.65A1-352[»]
ProteinModelPortaliO24529.
SMRiO24529. Positions 8-352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO24529.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni118 – 12710Substrate binding

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O24529-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSINGRKP SEIFKAQALL YKHIYAFIDS MSLKWAVEMN IPNIIQNHGK
60 70 80 90 100
PISLSNLVSI LQVPSSKIGN VRRLMRYLAH NGFFEIITKE EESYALTVAS
110 120 130 140 150
ELLVRGSDLC LAPMVECVLD PTLSGSYHEL KKWIYEEDLT LFGVTLGSGF
160 170 180 190 200
WDFLDKNPEY NTSFNDAMAS DSKLINLALR DCDFVFDGLE SIVDVGGGTG
210 220 230 240 250
TTAKIICETF PKLKCIVFDR PQVVENLSGS NNLTYVGGDM FTSIPNADAV
260 270 280 290 300
LLKYILHNWT DKDCLRILKK CKEAVTNDGK RGKVTIIDMV IDKKKDENQV
310 320 330 340 350
TQIKLLMDVN MACLNGKERN EEEWKKLFIE AGFQHYKISP LTGFLSLIEI

YP
Length:352
Mass (Da):39,604
Last modified:January 1, 1998 - v1
Checksum:i31B95228986C1296
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97125 mRNA. Translation: AAC49928.1.
PIRiT09707.

Genome annotation databases

KEGGiag:AAC49928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97125 mRNA. Translation: AAC49928.1.
PIRiT09707.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FP2X-ray1.40A1-352[»]
1FPXX-ray1.65A1-352[»]
ProteinModelPortaliO24529.
SMRiO24529. Positions 8-352.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC49928.

Enzyme and pathway databases

UniPathwayiUPA00902.
BRENDAi2.1.1.150. 3078.
2.1.1.270. 3078.

Miscellaneous databases

EvolutionaryTraceiO24529.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning and characterization of an elicitor-inducible isoflavone 7-O-methyltransferase."
    He X.-Z., Reddy J.T., Dixon R.A.
    Plant Mol. Biol. 36:43-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Affinity chromatography, substrate/product specificity, and amino acid sequence analysis of an isoflavone O-methyltransferase from alfalfa (Medicago sativa L.)."
    He X.-Z., Dixon R.A.
    Arch. Biochem. Biophys. 336:121-129(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-31; 77-105 AND 327-337, CHARACTERIZATION.
  3. "Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases."
    Zubieta C., He X.-Z., Dixon R.A., Noel J.P.
    Nat. Struct. Biol. 8:271-279(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, SUBUNIT.

Entry informationi

Entry namei7OMT8_MEDSA
AccessioniPrimary (citable) accession number: O24529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.