IAMT1_ORYSJ
ID IAMT1_ORYSJ Reviewed; 404 AA.
AC Q0J998; A0A0P0WGA0; Q7XPK4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Indole-3-acetate O-methyltransferase 1;
DE EC=2.1.1.278;
DE AltName: Full=IAA carboxylmethyltransferase 1;
DE AltName: Full=OsSABATH4;
DE AltName: Full=S-adenosyl-L-methionine:(indol-3-yl) acetate carboxylmethyltransferase 1;
GN Name=IAMT1; Synonyms=SABATH4;
GN OrderedLocusNames=Os04g0665200, LOC_Os04g56950; ORFNames=OSJNBa0087O24.5;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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. MeIAA seems to be an inactive form of IAA.
CC {ECO:0000269|PubMed:18162595}.
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:18162595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18162595};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and panicles.
CC {ECO:0000269|PubMed:18162595}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE03582.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU375746; ABZ04474.1; -; mRNA.
DR EMBL; AL606646; CAE03582.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008210; BAF16089.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91499.1; -; Genomic_DNA.
DR EMBL; AK110936; BAG99087.1; -; mRNA.
DR RefSeq; XP_015636829.1; XM_015781343.1.
DR RefSeq; XP_015636831.1; XM_015781345.1.
DR AlphaFoldDB; Q0J998; -.
DR SMR; Q0J998; -.
DR STRING; 4530.OS04T0665200-01; -.
DR PaxDb; Q0J998; -.
DR PRIDE; Q0J998; -.
DR EnsemblPlants; Os04t0665200-01; Os04t0665200-01; Os04g0665200.
DR GeneID; 4337315; -.
DR Gramene; Os04t0665200-01; Os04t0665200-01; Os04g0665200.
DR KEGG; osa:4337315; -.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_019628_1_1_1; -.
DR InParanoid; Q0J998; -.
DR OMA; SWAIQWL; -.
DR OrthoDB; 689338at2759; -.
DR BRENDA; 2.1.1.278; 8948.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q0J998; OS.
DR GO; GO:0051749; F:indole acetic acid carboxyl methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0103007; F:indole-3-acetate carboxyl methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0010252; P:auxin homeostasis; IC:UniProtKB.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
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 Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..404
FT /note="Indole-3-acetate O-methyltransferase 1"
FT /id="PRO_0000406603"
FT BINDING 82..83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 169..171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 404 AA; 43751 MW; 75971A9ADA49BC78 CRC64;
MTMAMASMKG ENVTVSAAAA PRMKKLASML CMKGGNGDGS YLNNSQAQAL HARRMLHFLE
ETLDAMMERS SSDKLFTAAD LGCSCGSNSL FIVDVIVRRV SEAYESRGRD APEFQVFFSD
LPSNDFNTLF QLLPPLLAPV AGSLEECLAA GEGAATATRP YHAAGVPGTF YGRLFPGESI
DVFTSTFSLH WLSQVPEEVG DSASPAYNGG RVFVHRATEA VAAAYKRQFQ ADLARFLRSR
AREMKRGGAM FLACLGRSSG DPADQGGAGL LFGTHFQDAW DDLVQEGVVE GEKRDSFNIP
VYAPSLQEFR DVVRADGAFA IDRLELVRGG SPLVVDRPDD AAEVGRAMAN SCKAVAGVLV
DAHIGERRGA QLFERLERRA ARHARELVEK MHFFHVVCSL SLAP
