AIMT1_PIMAN
ID AIMT1_PIMAN Reviewed; 358 AA.
AC B8RCD3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Trans-anol O-methyltransferase 1;
DE Short=T-anol O-methyltransferase 1;
DE EC=2.1.1.279;
DE AltName: Full=T-anol/isoeugenol O-methyltransferase 1;
DE Short=PaAIMT1;
GN Name=AIMT1;
OS Pimpinella anisum (Anise) (Anisum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Pimpinelleae; Pimpinella.
OX NCBI_TaxID=271192;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=18987218; DOI=10.1104/pp.108.128066;
RA Koeduka T., Baiga T.J., Noel J.P., Pichersky E.;
RT "Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol
RT synthase and an O-methyltransferase specific for a C7-C8 propenyl side
RT chain.";
RL Plant Physiol. 149:384-394(2009).
CC -!- FUNCTION: Phenylpropene O-methyltransferase that catalyzes the
CC conversion of trans-anol to trans-anethole and isoeugenol to
CC isomethyleugenol. Phenylpropenes are the primary constituents of
CC various essential plant oils. They are produced as antimicrobial and
CC antianimal compounds, or as floral attractants of pollinators.
CC {ECO:0000269|PubMed:18987218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + trans-anol = H(+) + S-adenosyl-L-
CC homocysteine + trans-anethole; Xref=Rhea:RHEA:36247,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:35616, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:73343; EC=2.1.1.279;
CC Evidence={ECO:0000269|PubMed:18987218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + trans-isoeugenol = H(+) + S-
CC adenosyl-L-homocysteine + trans-isomethyleugenol;
CC Xref=Rhea:RHEA:17081, ChEBI:CHEBI:6877, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:50545, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.279; Evidence={ECO:0000269|PubMed:18987218};
CC -!- ACTIVITY REGULATION: Inhibited by zinc and copper.
CC {ECO:0000269|PubMed:18987218}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.3 uM for isoeugenol (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:18987218};
CC KM=54.5 uM for S-adenosyl-L-methionine (at pH 7.5 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:18987218};
CC Note=kcat is 0.015 sec(-1) for isoeugenol.;
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:18987218};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing fruits. Expressed at
CC low levels in roots, young leaves, buds and flowers.
CC {ECO:0000269|PubMed:18987218}.
CC -!- MISCELLANEOUS: The phenylpropene trans-anethole imparts the
CC characteristic sweet aroma of anise seeds and leaves.
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; EU925389; ACL13527.1; -; mRNA.
DR AlphaFoldDB; B8RCD3; -.
DR SMR; B8RCD3; -.
DR KEGG; ag:ACL13527; -.
DR BioCyc; MetaCyc:MON-15433; -.
DR BRENDA; 2.1.1.279; 4840.
DR UniPathway; UPA00711; -.
DR GO; GO:0050630; F:(iso)eugenol O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Phenylpropanoid metabolism; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..358
FT /note="Trans-anol O-methyltransferase 1"
FT /id="PRO_0000424082"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 358 AA; 39629 MW; 481E8F1F5AE6F9DC CRC64;
MASHDQEAFL TAMQIVNSSA VDGVLICLIE LNVFDIMMQK AGMDGYLHPD EIALNLPTKN
PQAPEMLDRM LRILASHSII KCKLVKKMSG NALLTRAYGL TLISQYFVNA QDGPCLAPYL
KLIHHKQMQN SWEKVNEAVL EGGYAFNKAH AGSTFFEYLG KDKSVAELLS QTMAKSIPTS
MNILLKSYKG FEGVKEVVDV GGAYAATLSC IISFNPHVKG INFDVPHVIK NAPSLPGITH
VGGDMFESVP RGEAIVLQRV LHDWTDEESV KILKKCYEAI PDHGKVVIIE MIQTEMPEDD
IIAKNISEMD IRMLLYTPGG KERTVNEFLM LGKQAGFPSS KYICGADLYG VVELYKKK
