ANMT_RUTGR
ID ANMT_RUTGR Reviewed; 364 AA.
AC A9X7L0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Anthranilate N-methyltransferase;
DE Short=RgANMT;
DE EC=2.1.1.111;
OS Ruta graveolens (Common rue).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Rutoideae; Ruta.
OX NCBI_TaxID=37565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION BY ELICITOR, TISSUE
RP SPECIFICITY, MUTAGENESIS OF ASN-298, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=17988223; DOI=10.1111/j.1365-313x.2007.03360.x;
RA Rohde B., Hans J., Martens S., Baumert A., Hunziker P., Matern U.;
RT "Anthranilate N-methyltransferase, a branch-point enzyme of acridone
RT biosynthesis.";
RL Plant J. 53:541-553(2008).
CC -!- FUNCTION: Involved in the biosynthesis of acridine alkaloids. N-
CC methyltransferase with a strict substrate specificity for anthranilate.
CC No activity with anthranilic acid methyl ester, anthraniloyl CoA, 3- or
CC 4-amino-benzoic acid, salicylic acid, catechol, eugenol, caffeic acid,
CC quercetin, theobromin, theophyllin, putrescine and nicotinic acid among
CC others. {ECO:0000269|PubMed:17988223}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anthranilate + S-adenosyl-L-methionine = H(+) + N-
CC methylanthranilate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:12180,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:36557,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.111;
CC Evidence={ECO:0000269|PubMed:17988223};
CC -!- ACTIVITY REGULATION: Inhibited by Ca(2+), Co(2+), Fe(2+), Fe(3+),
CC Cu(2+) or Zn(2+). No effect of Mg(2+). {ECO:0000269|PubMed:17988223}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for anthranilate {ECO:0000269|PubMed:17988223};
CC KM=3.3 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:17988223};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17988223};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:17988223};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17988223}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, stems and roots.
CC Detected in the vascular tissues in stems, in the rhizodermis or the
CC endodermis of roots, in the inside of carpels, in the central vascular
CC bundles of the syncarp ovary and in the secretory oil glands located
CC around the outer ovary wall. {ECO:0000269|PubMed:17988223}.
CC -!- INDUCTION: Up-regulated by yeast elicitor treatment.
CC {ECO:0000269|PubMed:17988223}.
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; DQ884932; ABI93949.1; -; mRNA.
DR AlphaFoldDB; A9X7L0; -.
DR SMR; A9X7L0; -.
DR BioCyc; MetaCyc:MON-14024; -.
DR BRENDA; 2.1.1.111; 5486.
DR GO; GO:0030774; F:anthranilate N-methyltransferase activity; IEA:UniProtKB-EC.
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 Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..364
FT /note="Anthranilate N-methyltransferase"
FT /id="PRO_0000411115"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT MUTAGEN 298
FT /note="N->E: 150-fold decrease in catalytic efficiency but
FT substrate specificity unchanged."
FT /evidence="ECO:0000269|PubMed:17988223"
SQ SEQUENCE 364 AA; 40059 MW; 6F65F8AAE6152BD0 CRC64;
MGSLSESHTQ YKHGVEVEED EEESYSRAMQ LSMAIVLPMA TQSAIQLGVF EIIAKAPGGR
LSASEIATIL QAQNPKAPVM LDRMLRLLVS HRVLDCSVSG PAGERLYGLT SVSKYFVPDQ
DGASLGNFMA LPLDKVFMES WMGVKGAVME GGIPFNRVHG MHIFEYASSN SKFSDTYHRA
MFNHSTIALK RILEHYKGFE NVTKLVDVGG GLGVTLSMIA SKYPHIQAIN FDLPHVVQDA
ASYPGVEHVG GNMFESVPEG DAILMKWILH CWDDEQCLRI LKNCYKATPE NGKVIVMNSV
VPETPEVSSS ARETSLLDVL LMTRDGGGRE RTQKEFTELA IGAGFKGINF ACCVCNLHIM
EFFK
