KEGG   ENZYME: 2.1.1.278
Entry
EC 2.1.1.278                Enzyme                                 
Name
indole-3-acetate O-methyltransferase;
IAA carboxylmethyltransferase;
IAMT
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:(indol-3-yl)acetate O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + (indol-3-yl)acetate = S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate [RN:R10452]
Reaction(KEGG)
R10452
Substrate
S-adenosyl-L-methionine [CPD:C00019];
(indol-3-yl)acetate [CPD:C00954]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
methyl (indol-3-yl)acetate [CPD:C20635]
Comment
Binds Mg2+. The enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate. The product, methyl (indol-3-yl)acetate is inactive as hormone [2].
History
EC 2.1.1.278 created 2013
Orthology
K18848  indole-3-acetate O-methyltransferase
Genes
PCAN112574924
MYI110453983 110459980
LAK106152812 106152823
SPIS111319230
ATHAT5G55250(IAMT1)
ALY9300463
CRB17876787
CSAT104726072 104731592 104761558 109127202
EUSEUTSA_v10015669mg
BRP103844968
BNA106429974 125579158
BOE106314016
RSZ108827575
THJ104811634 104817688
CPAP110820813
CIT102609472
CICCICLE_v10008599mg
PVY116145152
MINC123192072 123201772 123202376
TCC18593419
GRA105781276
GHI107916882 107921728
GAB108481923
HSYR120126501 120145115 120160654 120202386
DZI111276433 111302246
EGR104448179 120294735
GMX100801476 100805902 100807953
GSJ114384238 114395612 114402697 114424307
PVUPHAVU_006G048600g PHAVU_008G272800g
VRA106764291 106774727
VAR108337490 108342409
VUN114187551 114193541
VUM124833035 124839492
CCAJ109806364 109811319
APRC113854354 113874579
MTR11425258 11435469 25489046
TPRA123916324 123918958 123920445
CAM101501068
PSAT127084846 127117629
VVO131617806 131646076 131656553
LJALj2g3v3222870.1(Lj2g3v3222870.1) Lj6g3v0819010.1(Lj6g3v0819010.1)
ADU107473281 107496314
AIP107606437 107616468
AHF112701906 112720225 112767332 112790358
LANG109329113 109350940 109359499
PCIN129299852 129317740
FVE101295605
RCN112167364
PPER18779912 18780210 18780650 18787700
PMUM103326506 103326551 103326552 103333170
PAVI110752403 110752586 110766633 110766652 110766659 110768917
PDUL117619897 117624998 117625448 117626244
MDM103428134 103448357
MSYL126589708 126614480
PXB103927001 103951421
ZJU107434320
MNT21395657
CSAV115725140
CSV101213472
CMO103490122
BHJ120085398
MCHA111010498 111010558
CMAX111476788 111480601
CMOS111442937 111445917
CPEP111788985 111797338
RCU8268129
JCU105633024
HBR110646361 110670024
MESC110601438 110610534
POP7487519
PEU105141854
PALZ118056815
JRE108983414 108992349
CILL122281509 122289623
CAVE132175306
QSU112029893
QLO115955000
TWL119985165 119989971
VVI100258858
VRI117910005
SLY101263921 101268451
SPEN107005882 107024610
SOT102590393 102598710
SSTN125862547 125875655
SDUL129870858 129893445
CANN107877415
LBB132617894 132619253 132638544
NTA107814352 107819865 107821105 107832655
NSY104225348 104233292
NTO104088383 104121023
NAU109208188 109226709
INI109187364 109190737
ITR116011409 116022530
SIND105174912
OEU111376492 111395122
EGT105969193
SSPL121756544 121756867 121786407
SMIL130986240
APAN127247786
HAN110890061
ECAD122593380
LSV111898207
CCAV112508026
DCR108216756
CSIN114280095 114321588
RVL131329600
AEW130751150 130771556
BVG104891752 104891754
SOE110777861
CQI110720881 110723927
ATRI130808095 130818297
MOF131164708
NNU104594143 104606532
MING122060482 122094202
TSS122640523 122641758
PSOM113285782 113333215
OSA107276275 4337315 4340899
DOSAOs04t0665200-01(Os04g0665200) Os06t0322400-00(Os06g0322400) Os06t0323100-01(Os06g0323100)
OBR102702090 102704052
OGL127771652 127777864
SVS117850524
PVIR120642779
PHAI112901107 112901210
PDA103702327
EGU105050524
MUS103995398 103995407
MSIN131219580
NCOL116259088
ATR18429711
MBRMONBRDRAFT_27501
SREPTSG_08577 PTSG_11672
MMAIsS8_3498
STARG3545_19560
PHRC6569_06540
 » show all
Reference
1  [PMID:12897246]
  Authors
Zubieta C, Ross JR, Koscheski P, Yang Y, Pichersky E, Noel JP
  Title
Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family.
  Journal
Plant Cell 15:1704-16 (2003)
DOI:10.1105/tpc.014548
  Sequence
[ath:AT5G55250]
Reference
2  [PMID:17926040]
  Authors
Li L, Hou X, Tsuge T, Ding M, Aoyama T, Oka A, Gu H, Zhao Y, Qu LJ
  Title
The possible action mechanisms of indole-3-acetic acid methyl ester in Arabidopsis.
  Journal
Plant Cell Rep 27:575-84 (2008)
DOI:10.1007/s00299-007-0458-9
  Sequence
[ath:AT5G55250]
Reference
3  [PMID:18162595]
  Authors
Zhao N, Ferrer JL, Ross J, Guan J, Yang Y, Pichersky E, Noel JP, Chen F
  Title
Structural, biochemical, and phylogenetic analyses suggest that indole-3-acetic acid methyltransferase is an evolutionarily ancient member of the SABATH family.
  Journal
Plant Physiol 146:455-67 (2008)
DOI:10.1104/pp.107.110049
  Sequence
[osa:4337315]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.278
IUBMB Enzyme Nomenclature: 2.1.1.278
ExPASy - ENZYME nomenclature database: 2.1.1.278
BRENDA, the Enzyme Database: 2.1.1.278

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