KEGG   ENZYME: 2.3.1.231Help
Entry
EC 2.3.1.231                Enzyme                                 

Name
tRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methoxycarbonyltransferase;
TYW4 (ambiguous);
tRNA-yW synthesizing enzyme-4 (ambiguous)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methyltransferase (carbon dioxide-adding)
Reaction(IUBMB)
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe + CO2 = S-adenosyl-L-homocysteine + wybutosine37 in tRNAPhe [RN:R10587]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe;
CO2 [CPD:C00011]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
wybutosine37 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-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.1.1.290, tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase [2].
History
EC 2.3.1.231 created 2013
Orthology
K15451  tRNA wybutosine-synthesizing protein 4
Genes
HSA: 9836(LCMT2)
PTR: 104002283(LCMT2)
PPS: 100976029(LCMT2)
GGO: 109023522(LCMT2)
PON: 100460816(LCMT2)
NLE: 100605890(LCMT2)
MCC: 710047(LCMT2)
MCF: 102138167(LCMT2)
CSAB: 103245741(LCMT2)
RRO: 104678484(LCMT2)
RBB: 108518286(LCMT2)
CJC: 100390904(LCMT2)
SBQ: 101043117(LCMT2)
MMU: 329504(Lcmt2)
RNO: 296098(Lcmt2)
CGE: 100768317(Lcmt2)
NGI: 103725087(Lcmt2)
HGL: 101718972(Lcmt2)
CCAN: 109682287(Lcmt2)
OCU: 100358713(LCMT2)
TUP: 102496763(LCMT2)
CFA: 100856672(LCMT2)
AML: 100474938(LCMT2)
UMR: 103673403(LCMT2)
ORO: 101379169(LCMT2)
FCA: 101100137(LCMT2)
PTG: 102967781(LCMT2)
AJU: 106968493(LCMT2)
BTA: 538825(LCMT2)
BOM: 102286559(LCMT2)
BIU: 109575422(LCMT2)
PHD: 102334078(LCMT2)
CHX: 102180973(LCMT2)
OAS: 101110182(LCMT2)
SSC: 100156590(LCMT2)
CFR: 102508672(LCMT2)
CDK: 105101728(LCMT2)
BACU: 102999234(LCMT2)
LVE: 103084551(LCMT2)
OOR: 101285867(LCMT2)
ECB: 100146685(LCMT2)
EPZ: 103556413(LCMT2)
EAI: 106835024(LCMT2)
MYB: 102246789(LCMT2)
MYD: 102752640(LCMT2)
HAI: 109383999(LCMT2)
RSS: 109442074 109444171(LCMT2)
PALE: 102882425(LCMT2)
LAV: 100677390(LCMT2)
TMU: 101354347
MDO: 107650707(LCMT2)
SHR: 100926867(LCMT2)
OAA: 100089395(LCMT2)
GGA: 419072(LCMT2)
MGP: 100549859(LCMT2)
CJO: 107308567(LCMT2)
APLA: 101790949(LCMT2)
ACYG: 106049772(LCMT2)
TGU: 100223696(LCMT2)
GFR: 102035314(LCMT2)
FAB: 101810513(LCMT2)
PHI: 102114241(LCMT2)
PMAJ: 107216417(LCMT2)
CCW: 104698084(LCMT2)
FPG: 101916966(LCMT2) 101920282
FCH: 102050993 102058812(LCMT2)
CLV: 102089517(LCMT2)
EGZ: 104130618(LCMT2)
AAM: 106497744(LCMT2)
ASN: 102377699(LCMT2)
AMJ: 102561035(LCMT2)
PSS: 102461808(LCMT2)
CMY: 102931256(LCMT2)
CPIC: 101950604(LCMT2)
ACS: 103282304(lcmt2)
PVT: 110078113(LCMT2)
PBI: 103063070(LCMT2)
GJA: 107116949(LCMT2)
XLA: 108711843
XTR: 100144923(lcmt2)
NPR: 108799881(LCMT2)
DRE: 100005300(lcmt2)
SRX: 107733625(lcmt2)
SGH: 107551959(lcmt2)
CCAR: 109096661(lcmt2)
IPU: 108266389(lcmt2)
AMEX: 103040183(lcmt2)
TRU: 101072307(lcmt2) 105419716
LCO: 104938167(lcmt2)
MZE: 101474934(lcmt2)
XMA: 102230549(lcmt2)
PRET: 103481866(lcmt2)
NFU: 107389574(lcmt2)
CSEM: 103391560(lcmt2)
LCF: 108902494(lcmt2)
HCQ: 109509607 109514521(lcmt2)
BPEC: 110170655(lcmt2)
SASA: 106586340(lcmt2)
ELS: 105016270(lcmt2)
SFM: 108922249(lcmt2)
LCM: 102353544(LCMT2)
CMK: 103182907(lcmt2)
CIN: 100181991
APLC: 110989265
SKO: 102806957
ZNE: 110839856
FCD: 110842720
CRG: 105343620
MYI: 110449727
OBI: 106871036
LAK: 106168044
EPA: 110255101
ADF: 107332030
HMG: 100197557
AQU: 100641360
ATH: AT1G02100(SBI1)
CRB: 17898295
BRP: 103843828
BOE: 106308422
THJ: 104801489
CPAP: 110810762
CIT: 102627581
TCC: 18614472
GRA: 105790311
EGR: 104441368
VRA: 106772101
VAR: 108340358
CAM: 101510447
ADU: 107486159
AIP: 107635262
LJA: Lj0g3v0203809.1(Lj0g3v0203809.1)
LANG: 109325163
FVE: 101315088
PPER: 18785493
PMUM: 103331617
CSV: 101210913
CMO: 103498812
MCHA: 111020748
RCU: 8265781
JCU: 105643220
HBR: 110635838
POP: 18105061
JRE: 109016645
VVI: 100251361
SLY: 101257704
SPEN: 107008230
SOT: 102598619
CANN: 107845277
NSY: 104242704
NTO: 104115518
INI: 109182849
SIND: 105173274
OEU: 111367085
HAN: 110900111
LSV: 111893281
DCR: 108203067
BVG: 104905270
SOE: 110803938
NNU: 104610492
OSA: 4340066
DOSA: Os06t0140100-01(Os06g0140100)
OBR: 102722682
BDI: 100830236
ATS: 109786856(LOC109786856)
SBI: 8070707
ZMA: 100282206(si605011g10)
SITA: 101780798
PDA: 103696854
EGU: 105061523
MUS: 103992952
DCT: 110107766
AOF: 109839467
ATR: 18428274
PPP: 112283989
APRO: F751_0856
SCE: YOL141W(PPM2)
NCS: NCAS_0C04370(NCAS0C04370)
NDI: NDAI_0G03760(NDAI0G03760)
TPF: TPHA_0P01530(TPHA0P01530)
TBL: TBLA_0H00180(TBLA0H00180)
TDL: TDEL_0A00340(TDEL0A00340)
KAF: KAFR_0I02910(KAFR0I02910)
PIC: PICST_80234(PPM2)
CAL: CAALFM_C101150CA(CaO19.3303)
CAUR: QG37_01806
SLB: AWJ20_3662(PPM2)
NCR: NCU05392
NTE: NEUTE1DRAFT123268(NEUTE1DRAFT_123268)
MGR: MGG_03140
MAW: MAC_08067
MAJ: MAA_05301
CMT: CCM_07440
BFU: BCIN_13g04270(Bcppm2)
MBE: MBM_09582
ANI: AN0128.2
ANG: ANI_1_1244164(An18g03060)
ABE: ARB_03109
TVE: TRV_05813
PTE: PTT_17719
DFA: DFA_06610
PYO: PY17X_1307400(PY00828)
PCB: PCHAS_130680(PC001098.02.0)
TPV: TP04_0135
BBO: BBOV_III003160(17.m07303)
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)
SPAR: SPRG_02835
 » 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 25:2142-54 (2006)
DOI:10.1038/sj.emboj.7601105
  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 37:2910-25 (2009)
DOI:10.1093/nar/gkp158
  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 39:1576-85 (2011)
DOI:10.1093/nar/gkq919
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.231
IUBMB Enzyme Nomenclature: 2.3.1.231
ExPASy - ENZYME nomenclature database: 2.3.1.231
BRENDA, the Enzyme Database: 2.3.1.231

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