KEGG   ENZYME: 2.1.1.290Help
Entry
EC 2.1.1.290                Enzyme                                 

Name
tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase;
TYW4 (ambiguous);
tRNA-yW synthesizing enzyme-4 (ambiguous)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-carboxypropyl]wyosine37-O}-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine37 in tRNAPhe = S-adenosyl-L-homocysteine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe [RN:R10586]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
7-[(3S)-3-amino-3-carboxypropyl]wyosine37 in tRNAPhe
Product
S-adenosyl-L-homocysteine [CPD:C00021];
7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe
Comment
The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.3.1.231, tRNAPhe 7-[(3S)-4-methoxy-(3-amino-3-carboxypropyl)wyosine37-O]-carbonyltransferase [2].
History
EC 2.1.1.290 created 2013
Orthology
K15451  
tRNA wybutosine-synthesizing protein 4
Genes
HSA: 
9836(LCMT2)
PTR: 
104002283(LCMT2)
PPS: 
100976029(LCMT2)
PON: 
100460816(LCMT2)
NLE: 
100605890(LCMT2)
MCC: 
710047(LCMT2)
MCF: 
102138167(LCMT2)
CSAB: 
103245741(LCMT2)
RRO: 
104678484(LCMT2)
CJC: 
100390904(LCMT2)
SBQ: 
101043117(LCMT2)
MMU: 
329504(Lcmt2)
RNO: 
296098(Lcmt2)
CGE: 
100768317(Lcmt2)
NGI: 
103725087(Lcmt2)
HGL: 
101718972(Lcmt2)
OCU: 
100358713(LCMT2)
TUP: 
102496763(LCMT2)
CFA: 
100856672(LCMT2)
AML: 
100474938(LCMT2)
UMR: 
103673403(LCMT2)
FCA: 
101100137(LCMT2)
PTG: 
102967781(LCMT2)
BTA: 
538825(LCMT2)
BOM: 
102286559(LCMT2)
PHD: 
102334078(LCMT2)
CHX: 
102180973(LCMT2)
OAS: 
101110182(LCMT2)
SSC: 
100156590(LCMT2)
CFR: 
102508672(LCMT2)
BACU: 
102999234(LCMT2)
LVE: 
103084551(LCMT2)
ECB: 
100146685(LCMT2)
MYB: 
102246789(LCMT2)
MYD: 
102752640(LCMT2)
PALE: 
102882425(LCMT2)
LAV: 
100677390(LCMT2)
MDO: 
107650707(LCMT2)
SHR: 
100926867(LCMT2)
OAA: 
100089395(LCMT2)
GGA: 
419072(LCMT2)
MGP: 
100549859(LCMT2)
CJO: 
107308567(LCMT2)
APLA: 
101790949(LCMT2)
TGU: 
100223696(LCMT2)
GFR: 
102035314(LCMT2)
FAB: 
101810513(LCMT2)
PHI: 
102114241(LCMT2)
CCW: 
104698084(LCMT2)
FPG: 
FCH: 
CLV: 
102089517(LCMT2)
AAM: 
106497744(LCMT2)
ASN: 
102377699(LCMT2)
AMJ: 
102561035(LCMT2)
PSS: 
102461808(LCMT2)
CMY: 
102931256(LCMT2)
ACS: 
103282304(lcmt2)
PBI: 
103063070(LCMT2)
GJA: 
107116949(LCMT2)
XTR: 
100144923(lcmt2)
DRE: 
100005300(lcmt2)
TRU: 
TNG: 
MZE: 
101474934(lcmt2)
OLA: 
XMA: 
102230549(lcmt2)
SASA: 
106586340(lcmt2)
LCM: 
102353544(LCMT2)
CMK: 
103182907(lcmt2)
CIN: 
SPU: 
SKO: 
PHU: 
DPX: 
ISC: 
HRO: 
LGI: 
CRG: 
OBI: 
NVE: 
ADF: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
EGR: 
GMX: 
PVU: 
VRA: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj0g3v0203809.1(Lj0g3v0203809.1)
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
VVI: 
SLY: 
SPEN: 
SOT: 
SIND: 
BVG: 
NNU: 
OSA: 
DOSA: 
Os06t0140100-01(Os06g0140100)
OBR: 
BDI: 
SBI: 
SORBI_10g002720(SORBIDRAFT_10g002720)
ZMA: 
100282206(si605011g10)
SITA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
CRE: 
VCN: 
MIS: 
MPP: 
CSL: 
CVR: 
APRO: 
GSL: 
CCP: 
SCE: 
YOL141W(PPM2)
AGO: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0C04370(NCAS0C04370)
NDI: 
NDAI_0G03760(NDAI0G03760)
TPF: 
TPHA_0P01530(TPHA0P01530)
TBL: 
TBLA_0H00180(TBLA0H00180)
TDL: 
TDEL_0A00340(TDEL0A00340)
KAF: 
KAFR_0I02910(KAFR0I02910)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
NTE: 
NEUTE1DRAFT123268(NEUTE1DRAFT_123268)
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
FGR: 
FPU: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
VDA: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_496094(AO090120000285)
ANG: 
ANI_1_1244164(An18g03060)
AFV: 
ACT: 
NFI: 
CIM: 
CPW: 
PBL: 
PBN: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
TML: 
SPO: 
PGR: 
MLR: 
MBR: 
SRE: 
DDI: 
DPP: 
DFA: 
ACAN: 
PFA: 
PFD: 
PFH: 
PYO: 
PCB: 
PBE: 
PKN: 
PVX: 
PCY: 
TAN: 
TPV: 
TOT: 
BEQ: 
BBO: 
BBOV_III003160(17.m07303)
TGO: 
TET: 
PTM: 
SMIN: 
v1.2.018262.t1(symbB.v1.2.018262.t1) v1.2.038056.t1(symbB.v1.2.038056.t1) v1.2.038056.t2(symbB.v1.2.038056.t2) v1.2.038056.t3(symbB.v1.2.038056.t3)
PIF: 
SPAR: 
EHX: 
GTT: 
TBR: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
 » show all
Taxonomy
Reference
1  [PMID:16642040]
  Authors
Noma A, Kirino Y, Ikeuchi Y, Suzuki T
  Title
Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA.
  Journal
EMBO. J. 25 (2006) 2142-54.
  Sequence
[sce:YOL141W]
Reference
2  [PMID:19287006]
  Authors
Suzuki Y, Noma A, Suzuki T, Ishitani R, Nureki O
  Title
Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4.
  Journal
Nucleic. Acids. Res. 37 (2009) 2910-25.
  Sequence
[sce:YOL141W]
Reference
3  [PMID:20972222]
  Authors
Kato M, Araiso Y, Noma A, Nagao A, Suzuki T, Ishitani R, Nureki O
  Title
Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification.
  Journal
Nucleic. Acids. Res. 39 (2011) 1576-85.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system