IGMT2_ARATH
ID IGMT2_ARATH Reviewed; 373 AA.
AC Q9LPU7; Q56XW7;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Indole glucosinolate O-methyltransferase 2 {ECO:0000303|PubMed:21317374};
DE EC=2.1.1.- {ECO:0000305};
GN Name=IGMT2 {ECO:0000303|PubMed:21317374};
GN OrderedLocusNames=At1g21120 {ECO:0000312|Araport:AT1G21120};
GN ORFNames=T22I11.5 {ECO:0000312|EMBL:AAF80649.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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).
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 -!- 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; AAF80649.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30066.1; -; Genomic_DNA.
DR EMBL; AF344315; AAK06866.1; -; mRNA.
DR EMBL; AK221556; BAD94958.1; -; mRNA.
DR PIR; D86344; D86344.
DR RefSeq; NP_001319057.1; NM_001332485.1.
DR AlphaFoldDB; Q9LPU7; -.
DR SMR; Q9LPU7; -.
DR STRING; 3702.AT1G21120.1; -.
DR PaxDb; Q9LPU7; -.
DR PRIDE; Q9LPU7; -.
DR ProteomicsDB; 228836; -.
DR EnsemblPlants; AT1G21120.1; AT1G21120.1; AT1G21120.
DR GeneID; 838708; -.
DR Gramene; AT1G21120.1; AT1G21120.1; AT1G21120.
DR KEGG; ath:AT1G21120; -.
DR Araport; AT1G21120; -.
DR TAIR; locus:2199587; AT1G21120.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_1_1; -.
DR InParanoid; Q9LPU7; -.
DR PhylomeDB; Q9LPU7; -.
DR BioCyc; ARA:AT1G21120-MON; -.
DR PRO; PR:Q9LPU7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPU7; 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:1990110; P:callus formation; IMP:TAIR.
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 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..373
FT /note="Indole glucosinolate O-methyltransferase 2"
FT /id="PRO_0000435496"
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"
FT CONFLICT 309
FT /note="T -> I (in Ref. 4; BAD94958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 40912 MW; 0E4378D35CC24091 CRC64;
MGYLFEETLS SNPKTPIVVD DDNELGLMAV RLANAAAFPM VLKASLELGV FDTLYAEASR
TDSFLSPSEI ASKLPTTPRN PGAPVLLDRM LRLLASYSMV KCEKVSVGKG ERVYRAEPIC
RFFLKNNIQD IGSLASQVIV NFDSVFLNTW AQLKDVVLEG GDAFGRAHGG MKLFDYMGTD
ERFSKLFNQT GFTIAVVKKA LEVYQGFKGV NVLVDVGGGV GNTLGVVTSK YPNIKGINFD
LTCALAQAPS YPGVEHVAGD MFVDVPTGDA MILKRILHDW TDEDCVKILK NCWKSLPENG
KVVVIELVTP DEAENGDINA NIAFDMDMLM FTQCSGGKER SRAEFEALAA ASCFTHCKFV
CQAYHCWIIE FCK
