Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Indole-3-acetate O-methyltransferase 1 (EC 2.1.1.278) (IAA carboxylmethyltransferase 1) (S-adenosyl-L-methionine:(indol-3-yl) acetate carboxylmethyltransferase 1)

 IAMT1_ARATH             Reviewed;         386 AA.
Q9FLN8; A8MS18; Q56ZV4; Q8LAR1;
05-APR-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-APR-2018, entry version 93.
RecName: Full=Indole-3-acetate O-methyltransferase 1;
EC=2.1.1.278;
AltName: Full=IAA carboxylmethyltransferase 1;
AltName: Full=S-adenosyl-L-methionine:(indol-3-yl) acetate carboxylmethyltransferase 1;
Name=IAMT1; OrderedLocusNames=At5g55250; ORFNames=MCO15.20;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12897246; DOI=10.1105/tpc.014548;
Zubieta C., Ross J.R., Koscheski P., Yang Y., Pichersky E., Noel J.P.;
"Structural basis for substrate recognition in the salicylic acid
carboxyl methyltransferase family.";
Plant Cell 15:1704-1716(2003).
[6]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16169896; DOI=10.1105/tpc.105.034959;
Qin G., Gu H., Zhao Y., Ma Z., Shi G., Yang Y., Pichersky E., Chen H.,
Liu M., Chen Z., Qu L.J.;
"An indole-3-acetic acid carboxyl methyltransferase regulates
Arabidopsis leaf development.";
Plant Cell 17:2693-2704(2005).
[7]
FUNCTION.
PubMed=17926040; DOI=10.1007/s00299-007-0458-9;
Li L., Hou X., Tsuge T., Ding M., Aoyama T., Oka A., Gu H., Zhao Y.,
Qu L.J.;
"The possible action mechanisms of indole-3-acetic acid methyl ester
in Arabidopsis.";
Plant Cell Rep. 27:575-584(2008).
[8]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 13-386 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE, COFACTOR, AND SUBUNIT.
PubMed=18162595; DOI=10.1104/pp.107.110049;
Zhao N., Ferrer J.L., Ross J., Guan J., Yang Y., Pichersky E.,
Noel J.P., Chen F.;
"Structural, biochemical, and phylogenetic analyses suggest that
indole-3-acetic acid methyltransferase is an evolutionarily ancient
member of the SABATH family.";
Plant Physiol. 146:455-467(2008).
-!- FUNCTION: Catalyzes the methylation of the free carboxyl end of
the plant hormone indole-3-acetic acid (IAA). Converts IAA to IAA
methyl ester (MeIAA). Regulates IAA activities by IAA methylation.
Methylation of IAA plays an important role in regulating plant
development and auxin homeostasis. Required for correct leaf
pattern formation. MeIAA seems to be an inactive form of IAA.
{ECO:0000269|PubMed:12897246, ECO:0000269|PubMed:16169896,
ECO:0000269|PubMed:17926040}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + (indol-3-yl)acetate
= S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate.
{ECO:0000269|PubMed:12897246}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:18162595};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000269|PubMed:18162595};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13 uM for indole-3-acetic acid (IAA)
{ECO:0000269|PubMed:12897246};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18162595}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9FLN8-1; Sequence=Displayed;
Name=2;
IsoId=Q9FLN8-2; Sequence=VSP_040835;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Expressed in seedling roots and leaves.
Expressed in the stigma, funiculus, and vascular bundles in
sepals, petals and stamens. {ECO:0000269|PubMed:16169896}.
-!- DEVELOPMENTAL STAGE: After the eighth true leaves emerge, the
expression gradually fades away from the center of the leaves
toward the edges, as leaf development proceedes. In fully expanded
leaves, expressed only at the edge of the leaf blade.
{ECO:0000269|PubMed:16169896}.
-!- MISCELLANEOUS: Plant silencing IAMT1 are smaller than the wild-
type, show epinastic leaves and smaller siliques, and have low
fertility. {ECO:0000305|PubMed:16169896}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. SABATH
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM65203.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB010071; BAB08594.1; -; Genomic_DNA.
EMBL; CP002688; AED96605.1; -; Genomic_DNA.
EMBL; CP002688; AED96606.1; -; Genomic_DNA.
EMBL; AK175586; BAD43349.1; -; mRNA.
EMBL; AK220857; BAD94212.1; -; mRNA.
EMBL; AK229885; BAF01714.1; -; mRNA.
EMBL; AY087665; AAM65203.1; ALT_INIT; mRNA.
RefSeq; NP_001078756.1; NM_001085287.2. [Q9FLN8-2]
RefSeq; NP_200336.1; NM_124907.5. [Q9FLN8-1]
UniGene; At.29454; -.
PDB; 3B5I; X-ray; 2.75 A; A/B=13-386.
PDBsum; 3B5I; -.
ProteinModelPortal; Q9FLN8; -.
SMR; Q9FLN8; -.
BioGrid; 20862; 1.
STRING; 3702.AT5G55250.1; -.
iPTMnet; Q9FLN8; -.
PaxDb; Q9FLN8; -.
EnsemblPlants; AT5G55250.1; AT5G55250.1; AT5G55250. [Q9FLN8-1]
EnsemblPlants; AT5G55250.2; AT5G55250.2; AT5G55250. [Q9FLN8-2]
GeneID; 835618; -.
Gramene; AT5G55250.1; AT5G55250.1; AT5G55250. [Q9FLN8-1]
Gramene; AT5G55250.2; AT5G55250.2; AT5G55250. [Q9FLN8-2]
KEGG; ath:AT5G55250; -.
Araport; AT5G55250; -.
TAIR; locus:2161680; AT5G55250.
eggNOG; ENOG410IIJ3; Eukaryota.
eggNOG; ENOG410Y96G; LUCA.
HOGENOM; HOG000238197; -.
InParanoid; Q9FLN8; -.
KO; K18848; -.
OMA; DAMMERS; -.
OrthoDB; EOG09360CRL; -.
PhylomeDB; Q9FLN8; -.
BioCyc; ARA:AT5G55250-MONOMER; -.
BRENDA; 2.1.1.278; 399.
EvolutionaryTrace; Q9FLN8; -.
PRO; PR:Q9FLN8; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FLN8; baseline and differential.
Genevisible; Q9FLN8; AT.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0051749; F:indole acetic acid carboxyl methyltransferase activity; IDA:TAIR.
GO; GO:0103007; F:indole-3-acetate carboxyl methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0010252; P:auxin homeostasis; IMP:UniProtKB.
GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IMP:TAIR.
InterPro; IPR005299; MeTrfase_7.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR31009; PTHR31009; 1.
Pfam; PF03492; Methyltransf_7; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Magnesium;
Metal-binding; Methyltransferase; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 386 Indole-3-acetate O-methyltransferase 1.
/FTId=PRO_0000406602.
REGION 33 37 Substrate binding.
{ECO:0000250|UniProtKB:A4GE69}.
REGION 72 73 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
REGION 108 111 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:A4GE70}.
REGION 152 154 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
REGION 169 171 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
REGION 170 174 Substrate binding.
{ECO:0000250|UniProtKB:A4GE70}.
METAL 191 191 Magnesium; via carbonyl oxygen.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
METAL 195 195 Magnesium; via amide nitrogen.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
METAL 277 277 Magnesium; via carbonyl oxygen.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
METAL 278 278 Magnesium; via carbonyl oxygen.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
METAL 280 280 Magnesium; via carbonyl oxygen.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
METAL 281 281 Magnesium. {ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
BINDING 30 30 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:A4GE70}.
BINDING 30 30 Substrate.
{ECO:0000250|UniProtKB:A4GE70}.
BINDING 72 72 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:A4GE69}.
BINDING 78 78 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
BINDING 110 110 S-adenosyl-L-methionine.
{ECO:0000244|PDB:3B5I,
ECO:0000269|PubMed:18162595}.
BINDING 334 334 Substrate.
{ECO:0000250|UniProtKB:A4GE69}.
VAR_SEQ 1 38 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_040835.
CONFLICT 68 68 A -> T (in Ref. 4; AAM65203).
{ECO:0000305}.
CONFLICT 241 241 T -> I (in Ref. 3; BAD94212/BAF01714).
{ECO:0000305}.
HELIX 41 53 {ECO:0000244|PDB:3B5I}.
STRAND 60 62 {ECO:0000244|PDB:3B5I}.
STRAND 66 71 {ECO:0000244|PDB:3B5I}.
HELIX 77 96 {ECO:0000244|PDB:3B5I}.
STRAND 104 110 {ECO:0000244|PDB:3B5I}.
HELIX 116 122 {ECO:0000244|PDB:3B5I}.
STRAND 144 151 {ECO:0000244|PDB:3B5I}.
STRAND 163 170 {ECO:0000244|PDB:3B5I}.
HELIX 180 183 {ECO:0000244|PDB:3B5I}.
TURN 192 194 {ECO:0000244|PDB:3B5I}.
STRAND 195 199 {ECO:0000244|PDB:3B5I}.
HELIX 202 226 {ECO:0000244|PDB:3B5I}.
STRAND 227 239 {ECO:0000244|PDB:3B5I}.
HELIX 249 255 {ECO:0000244|PDB:3B5I}.
HELIX 258 265 {ECO:0000244|PDB:3B5I}.
STRAND 268 272 {ECO:0000244|PDB:3B5I}.
HELIX 274 277 {ECO:0000244|PDB:3B5I}.
HELIX 289 299 {ECO:0000244|PDB:3B5I}.
STRAND 301 311 {ECO:0000244|PDB:3B5I}.
HELIX 324 344 {ECO:0000244|PDB:3B5I}.
HELIX 349 365 {ECO:0000244|PDB:3B5I}.
HELIX 368 371 {ECO:0000244|PDB:3B5I}.
STRAND 377 385 {ECO:0000244|PDB:3B5I}.
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


Related products :

Catalog number Product name Quantity
26-321 TRMT11 belongs to the methyltransferase superfamily. It is a catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nuc 0.05 mg
30-422 TRMT11 belongs to the methyltransferase superfamily. It is a catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nuc 0.05 mg
26-374 METT5D1 belongs to the methyltransferase superfamily, mraW family. METT5D1 is a probable S-adenosyl-L-methionine-dependent methyltransferase. 0.05 mg
102415-39-4 Methyl Indole-2,4,5,6,7-D5-3-acetate [2H5]Indole-3-Acetic ac 1g
1544-5 Phorbol-12-myristate 13-acetate (PMA) PMA, 12-O-Tetradecanoylphorbol 13-acetate,TPA, 4β,9α,12β,13α,20-Pentahydroxytiglia-1,6-dien-3-one 12-tetradecanoate 13-acetate 5 mg
30-465 NSUN3 belongs to the methyltransferase superfamily. RsmB_NOP family. It may have S-adenosyl-L-methionine-dependent methyl-transferase activity. 0.05 mg
97540-22-2 S-Adenosyl-5-L-methionine tosylate S-Adenosyl Methionine 1g
29-083 TFB2M is a S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. It is also required for basal transcription of mitocho 0.1 mg
28-102 TFB2M is a S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. It is also required for basal transcription of mitocho 0.1 mg
71914-80-2 S-Adenosyl-L-methionine tosylate S-Adenosyl-L-methioni 1g
24346-00-7 S-Adenosyl-L-methionine chloride S-Adenosyl-L-methioni 1g
M313475 Methyl Indole-3-acetate C11H11NO2 CAS: 1912-33-0 500 mg
29-523 NSUN6 may have S-adenosyl-L-methionine-dependent methyl-transferase activity (Potential). NSUN6 belongs to the methyltransferase superfamily, RsmB_NOP family. It contains 1 PUA domain.Western blots us 0.05 mg
29-522 NSUN6 may have S-adenosyl-L-methionine-dependent methyl-transferase activity (Potential). NSUN6 belongs to the methyltransferase superfamily, RsmB_NOP family. It contains 1 PUA domain.Western blots us 0.05 mg
A-00233 3-ACETOXY INDOLE (Indoxyl Acetate) (Store in Refrigerator) CAS: 608-08-2 5 gm
A-00233 3-ACETOXY INDOLE (Indoxyl Acetate) (Store in Refrigerator) CAS: 608-08-2 1 gm
A618001 3-Amino-1-methyl-5H-pyrido[4,3-b]indole Acetate C14H15N3O2 CAS: 72254-58-1 10 mg
A607502 3-Amino-1,4-dimethyl-5H-pyrido[4,3-b]indole-13C2,15N Acetate C1313C2H17N215NO2 CAS: 0.5 mg
A618002 3-Amino-1-methyl-5H-pyrido[4,3-b]indole-13C2,15N Acetate C1213C2H15N215NO2 CAS: 1 mg
A607500 3-Amino-1,4-dimethyl-5H-pyrido[4,3-b]indole Acetate C15H17N3O2 CAS: 68808-54-8 10 mg
orb80754 Salmon Calcitonin Acetate protein Calcitonin Acetate (Salmon) is synthetic polypeptide of 32 amino acids in the same linear sequencethat is found in clacitonin of salmon origin. Calcitonin Acetate (Sa 1 mg
orb41194 WBSCR22 antibody Polyclonal Rabbit polyclonal to WBSCR22. This gene encodes a protein containing a nuclear localization signal and an S-adenosyl-L-methionine binding motif typical of methyltransferase 100
12201-55 Diethylene Glycol Monoethyl Ether Acetate 〔2‐(2‐Ethoxyethoxy)ethyl Acetate〕 CAS: 112-15-2 500ML
12201-55 Diethylene Glycol Monoethyl Ether Acetate 〔2‐(2‐Ethoxyethoxy)ethyl Acetate〕 500ML
12120-44 Diethylene Glycol Monobutyl Ether Acetate 〔2‐(2‐Butoxyethoxy)ethyl Acetate〕 15KG


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur