AMNMT_HORVV
ID AMNMT_HORVV Reviewed; 376 AA.
AC Q96565; Q42834;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=3-aminomethylindole N-methyltransferase {ECO:0000305};
DE EC=2.1.1.340 {ECO:0000269|PubMed:16664431, ECO:0000269|PubMed:16930646};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY JASMONIC ACID, AND
RP MISCELLANEOUS.
RC STRAIN=cv. Igri, cv. Morex, and cv. Salome;
RX PubMed=9524816; DOI=10.3109/10425179709034056;
RA Lee J.E., Kleinhofs A., Graner A., Wegener S., Parthier B., Loebler M.;
RT "Genomic sequence and mapping of a methyljasmonate-induced O-
RT methyltransferase from barley (Hordeum vulgare L.).";
RL DNA Seq. 7:357-363(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Haruna Nijo; TISSUE=Shoot;
RX PubMed=21415278; DOI=10.1104/pp.110.171579;
RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA Sato K.;
RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT from 12 clone libraries.";
RL Plant Physiol. 156:20-28(2011).
RN [3]
RP INDUCTION BY HIGH TEMPERATURES, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=cv. Arimar, and cv. Proctor;
RX PubMed=16664431; DOI=10.1104/pp.79.2.451;
RA Leland T.J., Hanson A.D.;
RT "Induction of a specific N-Methyltransferase enzyme by long-term heat
RT stress during barley leaf growth.";
RL Plant Physiol. 79:451-457(1985).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP MISCELLANEOUS.
RC STRAIN=cv. 5172-28:4, cv. 5172-39:9, cv. 5175-50:20, cv. Barke,
RC cv. CI 11506, cv. CI 16145, cv. Golf,
RC cv. Hordeum vulgare ssp. spontaneum accession 5, cv. Lina, cv. Maythorpe,
RC cv. Mona, cv. Morex, and cv. Osiris;
RX PubMed=16930646; DOI=10.1016/j.phytochem.2006.06.036;
RA Larsson K.A.E., Zetterlund I., Delp G., Jonsson L.M.V.;
RT "N-Methyltransferase involved in gramine biosynthesis in barley: cloning
RT and characterization.";
RL Phytochemistry 67:2002-2008(2006).
CC -!- FUNCTION: Methylates 3-aminomethylindole (AMI) and N-methyl-3-
CC aminomethylindole (MAMI), two substrates involved in gramine
CC biosynthesis, a toxic indole alkaloid. Can use S-adenosyl-L-methionine
CC (AdoMet) as a methyl donor. Unable to mediate caffeic acid O-
CC methylation. {ECO:0000269|PubMed:16930646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(aminomethyl)indole + 2 S-adenosyl-L-methionine = gramine +
CC 2 H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:52264,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:136514, ChEBI:CHEBI:136516; EC=2.1.1.340;
CC Evidence={ECO:0000269|PubMed:16664431, ECO:0000269|PubMed:16930646};
CC -!- ACTIVITY REGULATION: Repressed by sodium carbonate, sodium bicarbonate
CC and K-phosphate. {ECO:0000269|PubMed:16664431}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77 uM for 3-aminomethylindole {ECO:0000269|PubMed:16930646};
CC KM=184 uM for N-methyl-3-aminomethylindole
CC {ECO:0000269|PubMed:16930646};
CC KM=148 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:16930646};
CC Vmax=37.21 pmol/sec/mg enzyme with 3-aminomethylindole as substrate
CC {ECO:0000269|PubMed:16930646};
CC Vmax=43.54 pmol/sec/mg enzyme with N-methyl-3-aminomethylindole as
CC substrate {ECO:0000269|PubMed:16930646};
CC Vmax=14.50 pmol/sec/mg enzyme with S-adenosylmethionine as substrate
CC {ECO:0000269|PubMed:16930646};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:16664431};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:16930646}.
CC -!- TISSUE SPECIFICITY: More present in the fifth leaf than in the second
CC leaf (at protein level). {ECO:0000269|PubMed:16664431}.
CC -!- INDUCTION: Induced by jasmonic acid (PubMed:9524816). Triggered by high
CC temperatures; 35 degrees Celsius day/30 degrees Celsius night (at
CC protein level) (PubMed:16664431). {ECO:0000269|PubMed:16664431,
CC ECO:0000269|PubMed:9524816}.
CC -!- MISCELLANEOUS: Present and expressed only in cultivars containing
CC gramine (e.g. cv. 5172-28:4, cv. 5172-39:9, cv. 5175-50:20, cv. Hordeum
CC vulgare ssp. spontaneum accession 5, cv. Golf, cv. Lina, cv. Barke, cv.
CC Sultan5, cv. Igri, cv. Salome and cv. Osiris) but not detected in cv.
CC CI 16145, cv. CI 11506, cv. Mona, cv. Morex and cv. Maythorpe.
CC {ECO:0000269|PubMed:16930646, ECO:0000269|PubMed:9524816}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; U54767; AAC18643.1; -; Genomic_DNA.
DR EMBL; AK353678; BAJ84897.1; -; mRNA.
DR PIR; T06189; T06189.
DR AlphaFoldDB; Q96565; -.
DR SMR; Q96565; -.
DR KEGG; ag:AAC18643; -.
DR BioCyc; MetaCyc:MON-12933; -.
DR BRENDA; 2.1.1.340; 2683.
DR Proteomes; UP000011116; Unassembled WGS sequence.
DR GO; GO:0102913; F:3-aminomethylindole N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..376
FT /note="3-aminomethylindole N-methyltransferase"
FT /id="PRO_0000442940"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
SQ SEQUENCE 376 AA; 41084 MW; DAF1B3B6CB0665C7 CRC64;
MDKISAPFFS GTSPAAASVA GVDEDDRLCF QAQELMFAYN ISMVLRAAIQ LGLLDALSAA
GGKALTPNEL VENVETSSNK AEAAAAVDRI LRYLSCFNVV TCSSEAAGPD GTLVRRYTTG
PLCRWLTKDR GDGTLSPFAV FVVDPDHLFP WHHIAEAVTA GGPSAFERTQ KWPYYEYMGK
NQRLGTLFDN AMAQHSVILV TKMLERFKGF DGVQRLVDVG GGTGSTLGMI TSKYKHMTGI
NYDLPHVIAQ GLPLPGVEHV AGDMYESIPT GDAVLLQWIT LMLNDDEFVK ILSNCHNALP
KDGKVIVVDG ILPENPDSSL TARDAFTLDI IMFVLFKGAK QRTEKEFARL AKQAGFTGGI
KKTYIFFNFY ALEFTK
