IGMT5_ARATH
ID IGMT5_ARATH Reviewed; 367 AA.
AC Q9SRD4; Q8L931;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Indole glucosinolate O-methyltransferase 5 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
GN Name=IGMT5 {ECO:0000305};
GN OrderedLocusNames=At1g76790 {ECO:0000312|Araport:AT1G76790};
GN ORFNames=F28O16.16 {ECO:0000312|EMBL:AAF04440.1};
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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, respectively. {ECO:0000250|UniProtKB:Q9LPU5}.
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM66988.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC010718; AAF04440.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35889.1; -; Genomic_DNA.
DR EMBL; BT002952; AAO22765.1; -; mRNA.
DR EMBL; BT004388; AAO42382.1; -; mRNA.
DR EMBL; AY088666; AAM66988.1; ALT_INIT; mRNA.
DR PIR; E96796; E96796.
DR RefSeq; NP_177805.1; NM_106329.3.
DR AlphaFoldDB; Q9SRD4; -.
DR SMR; Q9SRD4; -.
DR STRING; 3702.AT1G76790.1; -.
DR MetOSite; Q9SRD4; -.
DR PaxDb; Q9SRD4; -.
DR PRIDE; Q9SRD4; -.
DR ProteomicsDB; 228882; -.
DR EnsemblPlants; AT1G76790.1; AT1G76790.1; AT1G76790.
DR GeneID; 844013; -.
DR Gramene; AT1G76790.1; AT1G76790.1; AT1G76790.
DR KEGG; ath:AT1G76790; -.
DR Araport; AT1G76790; -.
DR TAIR; locus:2030081; AT1G76790.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_12_1_1; -.
DR InParanoid; Q9SRD4; -.
DR OMA; CKWLAGG; -.
DR OrthoDB; 817726at2759; -.
DR PhylomeDB; Q9SRD4; -.
DR BioCyc; ARA:AT1G76790-MON; -.
DR PRO; PR:Q9SRD4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRD4; baseline and differential.
DR GO; GO:0008171; F:O-methyltransferase activity; IMP:TAIR.
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:0009759; P:indole glucosinolate biosynthetic process; IMP: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..367
FT /note="Indole glucosinolate O-methyltransferase 5"
FT /id="PRO_0000435499"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 232
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 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT CONFLICT 63
FT /note="E -> D (in Ref. 4; AAM66988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40222 MW; B92F0AEEF38BC8CC CRC64;
MGHLIPQTGD EETELGLAAV RLANCAAFPM VFKAAIELGV IDTLYLAARD DVTGSSSFLT
PSEIAIRLPT KPSNPEAPAL LDRILRLLAS YSMVKCQIID GNRVYKAEPI CRYFLKDNVD
EELGTLASQL IVTLDTVFLN TWGELKNVVL EGGVAFGRAN GGLKLFDYIS KDERLSKLFN
RTGFSVAVLK KILQVYSGFE GVNVLVDVGG GVGDTLGFVT SKYPNIKGIN FDLTCALTQA
PSYPNVEHVA GDMFVDVPKG DAILLKRILH DWTDEDCEKI LKNCWKALPE NGKVIVMEVV
TPDEADNRDV ISNIAFDMDL LMLTQLSGGK ERSRAEYVAM AANSGFPRCN FVCSAYHLWV
IELTKQA
