IGMT1_ARATH
ID IGMT1_ARATH Reviewed; 373 AA.
AC Q9LPU5;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Indole glucosinolate O-methyltransferase 1 {ECO:0000303|PubMed:21317374};
DE EC=2.1.1.- {ECO:0000305};
GN Name=IGMT1 {ECO:0000303|PubMed:21317374};
GN OrderedLocusNames=At1g21100 {ECO:0000312|Araport:AT1G21100};
GN ORFNames=T22I11.7 {ECO:0000312|EMBL:AAF80651.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INDUCTION BY APHID.
RX PubMed=16167763; DOI=10.1094/mpmi-18-0923;
RA De Vos M., Van Oosten V.R., Van Poecke R.M., Van Pelt J.A., Pozo M.J.,
RA Mueller M.J., Buchala A.J., Metraux J.P., Van Loon L.C., Dicke M.,
RA Pieterse C.M.;
RT "Signal signature and transcriptome changes of Arabidopsis during pathogen
RT and insect attack.";
RL Mol. Plant Microbe Interact. 18:923-937(2005).
RN [5]
RP FUNCTION.
RX PubMed=21317374; DOI=10.1105/tpc.110.081711;
RA Pfalz M., Mikkelsen M.D., Bednarek P., Olsen C.E., Halkier B.A.,
RA Kroymann J.;
RT "Metabolic engineering in Nicotiana benthamiana reveals key enzyme
RT functions in Arabidopsis indole glucosinolate modification.";
RL Plant Cell 23:716-729(2011).
RN [6]
RP INTERACTION WITH B'GAMMA.
RX PubMed=27598402; DOI=10.1111/tpj.13326;
RA Rahikainen M., Trotta A., Alegre S., Pascual J., Vuorinen K., Overmyer K.,
RA Moffatt B., Ravanel S., Glawischnig E., Kangasjaervi S.;
RT "PP2A-B'gamma modulates foliar trans-methylation capacity and the formation
RT of 4-methoxy-indol-3-yl-methyl glucosinolate in Arabidopsis leaves.";
RL Plant J. 89:112-127(2017).
CC -!- FUNCTION: Involved in indole glucosinolate biosynthesis. Catalyzes
CC methoxylation reactions of the glucosinolate indole ring. Converts the
CC hydroxy intermediates 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-
CC I3M) and 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) to 4-
CC methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-
CC yl-methylglucosinolate (1MO-I3M), respectively.
CC {ECO:0000269|PubMed:21317374}.
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with B'GAMMA. {ECO:0000269|PubMed:27598402}.
CC -!- INDUCTION: By the green peach aphid Myzus persicae.
CC {ECO:0000269|PubMed:16167763}.
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; AC012190; AAF80651.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30064.1; -; Genomic_DNA.
DR EMBL; AF344316; AAK06867.1; -; mRNA.
DR EMBL; AY057529; AAL09769.1; -; mRNA.
DR EMBL; AY143974; AAN28913.1; -; mRNA.
DR PIR; B86344; B86344.
DR RefSeq; NP_173534.1; NM_101964.3.
DR AlphaFoldDB; Q9LPU5; -.
DR SMR; Q9LPU5; -.
DR STRING; 3702.AT1G21100.1; -.
DR PaxDb; Q9LPU5; -.
DR PRIDE; Q9LPU5; -.
DR ProteomicsDB; 232279; -.
DR EnsemblPlants; AT1G21100.1; AT1G21100.1; AT1G21100.
DR GeneID; 838706; -.
DR Gramene; AT1G21100.1; AT1G21100.1; AT1G21100.
DR KEGG; ath:AT1G21100; -.
DR Araport; AT1G21100; -.
DR TAIR; locus:2199607; AT1G21100.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_1_1; -.
DR InParanoid; Q9LPU5; -.
DR OMA; HHIKGIN; -.
DR OrthoDB; 817726at2759; -.
DR PhylomeDB; Q9LPU5; -.
DR BioCyc; ARA:AT1G21100-MON; -.
DR PRO; PR:Q9LPU5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPU5; baseline and differential.
DR GO; GO:0008168; F:methyltransferase activity; IDA:TAIR.
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:0042343; P:indole glucosinolate metabolic process; IDA:TAIR.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
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..373
FT /note="Indole glucosinolate O-methyltransferase 1"
FT /id="PRO_0000435495"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
SQ SEQUENCE 373 AA; 40869 MW; 3E4BADB35750B197 CRC64;
MGYLFQETLS SNPKTPIVVD DDNELGLMAV RLANAAAFPM VLKAALELGV FDTLYAAASR
TDSFLSPYEI ASKLPTTPRN PEAPVLLDRM LRLLASYSMV KCGKALSGKG ERVYRAEPIC
RFFLKDNIQD IGSLASQVIV NFDSVFLNTW AQLKDVVLEG GDAFGRAHGG MKLFDYMGTD
ERFSKLFNQT GFTIAVVKKA LEVYEGFKGV KVLVDVGGGV GNTLGVVTSK YPNIKGINFD
LTCALAQAPS YPGVEHVAGD MFVDVPTGDA MILKRILHDW TDEDCVKILK NCWKSLPENG
KVVVIELVTP DEAENGDINA NIAFDMDMLM FTQCSGGKER SRAEFEALAA ASGFTHCKFV
CQAYHCWIIE FCK
