IAMT1_ARATH
ID IAMT1_ARATH Reviewed; 386 AA.
AC Q9FLN8; A8MS18; Q56ZV4; Q8LAR1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Indole-3-acetate O-methyltransferase 1;
DE EC=2.1.1.278;
DE AltName: Full=IAA carboxylmethyltransferase 1;
DE AltName: Full=S-adenosyl-L-methionine:(indol-3-yl) acetate carboxylmethyltransferase 1;
GN Name=IAMT1; OrderedLocusNames=At5g55250; ORFNames=MCO15.20;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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] (ISOFORM 1).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12897246; DOI=10.1105/tpc.014548;
RA Zubieta C., Ross J.R., Koscheski P., Yang Y., Pichersky E., Noel J.P.;
RT "Structural basis for substrate recognition in the salicylic acid carboxyl
RT methyltransferase family.";
RL Plant Cell 15:1704-1716(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16169896; DOI=10.1105/tpc.105.034959;
RA Qin G., Gu H., Zhao Y., Ma Z., Shi G., Yang Y., Pichersky E., Chen H.,
RA Liu M., Chen Z., Qu L.J.;
RT "An indole-3-acetic acid carboxyl methyltransferase regulates Arabidopsis
RT leaf development.";
RL Plant Cell 17:2693-2704(2005).
RN [7]
RP FUNCTION.
RX PubMed=17926040; DOI=10.1007/s00299-007-0458-9;
RA Li L., Hou X., Tsuge T., Ding M., Aoyama T., Oka A., Gu H., Zhao Y.,
RA Qu L.J.;
RT "The possible action mechanisms of indole-3-acetic acid methyl ester in
RT Arabidopsis.";
RL Plant Cell Rep. 27:575-584(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 13-386 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, COFACTOR, AND SUBUNIT.
RX PubMed=18162595; DOI=10.1104/pp.107.110049;
RA Zhao N., Ferrer J.L., Ross J., Guan J., Yang Y., Pichersky E., Noel J.P.,
RA Chen F.;
RT "Structural, biochemical, and phylogenetic analyses suggest that indole-3-
RT acetic acid methyltransferase is an evolutionarily ancient member of the
RT SABATH family.";
RL Plant Physiol. 146:455-467(2008).
CC -!- FUNCTION: Catalyzes the methylation of the free carboxyl end of the
CC plant hormone indole-3-acetic acid (IAA). Converts IAA to IAA methyl
CC ester (MeIAA). Regulates IAA activities by IAA methylation. Methylation
CC of IAA plays an important role in regulating plant development and
CC auxin homeostasis. Required for correct leaf pattern formation. MeIAA
CC seems to be an inactive form of IAA. {ECO:0000269|PubMed:12897246,
CC ECO:0000269|PubMed:16169896, ECO:0000269|PubMed:17926040}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(indol-3-yl)acetate + S-adenosyl-L-methionine = methyl (indol-
CC 3-yl)acetate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36131,
CC ChEBI:CHEBI:30854, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:72782; EC=2.1.1.278;
CC Evidence={ECO:0000269|PubMed:12897246};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18162595};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:18162595};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for indole-3-acetic acid (IAA)
CC {ECO:0000269|PubMed:12897246};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18162595}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FLN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FLN8-2; Sequence=VSP_040835;
CC -!- TISSUE SPECIFICITY: Expressed in seedling roots and leaves. Expressed
CC in the stigma, funiculus, and vascular bundles in sepals, petals and
CC stamens. {ECO:0000269|PubMed:16169896}.
CC -!- DEVELOPMENTAL STAGE: After the eighth true leaves emerge, the
CC expression gradually fades away from the center of the leaves toward
CC the edges, as leaf development proceedes. In fully expanded leaves,
CC expressed only at the edge of the leaf blade.
CC {ECO:0000269|PubMed:16169896}.
CC -!- MISCELLANEOUS: Plant silencing IAMT1 are smaller than the wild-type,
CC show epinastic leaves and smaller siliques, and have low fertility.
CC {ECO:0000305|PubMed:16169896}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65203.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB010071; BAB08594.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96605.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96606.1; -; Genomic_DNA.
DR EMBL; AK175586; BAD43349.1; -; mRNA.
DR EMBL; AK220857; BAD94212.1; -; mRNA.
DR EMBL; AK229885; BAF01714.1; -; mRNA.
DR EMBL; AY087665; AAM65203.1; ALT_INIT; mRNA.
DR RefSeq; NP_001078756.1; NM_001085287.2. [Q9FLN8-2]
DR RefSeq; NP_200336.1; NM_124907.5. [Q9FLN8-1]
DR PDB; 3B5I; X-ray; 2.75 A; A/B=13-386.
DR PDBsum; 3B5I; -.
DR AlphaFoldDB; Q9FLN8; -.
DR SMR; Q9FLN8; -.
DR BioGRID; 20862; 1.
DR STRING; 3702.AT5G55250.1; -.
DR iPTMnet; Q9FLN8; -.
DR PaxDb; Q9FLN8; -.
DR PRIDE; Q9FLN8; -.
DR ProteomicsDB; 232192; -. [Q9FLN8-1]
DR EnsemblPlants; AT5G55250.1; AT5G55250.1; AT5G55250. [Q9FLN8-1]
DR EnsemblPlants; AT5G55250.2; AT5G55250.2; AT5G55250. [Q9FLN8-2]
DR GeneID; 835618; -.
DR Gramene; AT5G55250.1; AT5G55250.1; AT5G55250. [Q9FLN8-1]
DR Gramene; AT5G55250.2; AT5G55250.2; AT5G55250. [Q9FLN8-2]
DR KEGG; ath:AT5G55250; -.
DR Araport; AT5G55250; -.
DR TAIR; locus:2161680; AT5G55250.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_019628_1_1_1; -.
DR InParanoid; Q9FLN8; -.
DR OMA; SWAIQWL; -.
DR OrthoDB; 689338at2759; -.
DR PhylomeDB; Q9FLN8; -.
DR BioCyc; ARA:AT5G55250-MON; -.
DR BRENDA; 2.1.1.278; 399.
DR SABIO-RK; Q9FLN8; -.
DR EvolutionaryTrace; Q9FLN8; -.
DR PRO; PR:Q9FLN8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLN8; baseline and differential.
DR Genevisible; Q9FLN8; AT.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0051749; F:indole acetic acid carboxyl methyltransferase activity; IDA:TAIR.
DR GO; GO:0103007; F:indole-3-acetate carboxyl methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0010252; P:auxin homeostasis; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IMP:TAIR.
DR DisProt; DP02696; -.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Magnesium; Metal-binding;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..386
FT /note="Indole-3-acetate O-methyltransferase 1"
FT /id="PRO_0000406602"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 33..37
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 72..73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 108..111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 152..154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 169..171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 170..174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18162595,
FT ECO:0007744|PDB:3B5I"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040835"
FT CONFLICT 68
FT /note="A -> T (in Ref. 4; AAM65203)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="T -> I (in Ref. 3; BAD94212/BAF01714)"
FT /evidence="ECO:0000305"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 77..96
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3B5I"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 202..226
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 227..239
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 324..344
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 349..365
FT /evidence="ECO:0007829|PDB:3B5I"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:3B5I"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:3B5I"
SQ SEQUENCE 386 AA; 42054 MW; 10C0B025C4DEBE06 CRC64;
MGSKGDNVAV CNMKLERLLS MKGGKGQDSY ANNSQAQAMH ARSMLHLLEE TLENVHLNSS
ASPPPFTAVD LGCSSGANTV HIIDFIVKHI SKRFDAAGID PPEFTAFFSD LPSNDFNTLF
QLLPPLVSNT CMEECLAADG NRSYFVAGVP GSFYRRLFPA RTIDFFHSAF SLHWLSQVPE
SVTDRRSAAY NRGRVFIHGA GEKTTTAYKR QFQADLAEFL RARAAEVKRG GAMFLVCLGR
TSVDPTDQGG AGLLFGTHFQ DAWDDLVREG LVAAEKRDGF NIPVYAPSLQ DFKEVVDANG
SFAIDKLVVY KGGSPLVVNE PDDASEVGRA FASSCRSVAG VLVEAHIGEE LSNKLFSRVE
SRATSHAKDV LVNLQFFHIV ASLSFT
