Entry
Name
tRNA 4-demethylwyosine synthase (AdoMet-dependent);
TYW1
Class
Lyases;
Carbon-carbon lyases;
Oxo-acid-lyases
BRITE hierarchy
Sysname
tRNAPhe N1-methylguanine,pyruvate acetaldehyde-lyase (tRNAPhe 4-demethylwyosine-forming, decarboxylating, dehydrating)
Reaction(IUBMB)
N1-methylguanine37 in tRNAPhe + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine37 in tRNAPhe + L-methionine + 5'-deoxyadenosine + CO2 + H2O [RN:
R10552 ]
Reaction(KEGG)
Substrate
N1-methylguanine37 in tRNAPhe;
pyruvate [CPD:
C00022 ];
S-adenosyl-L-methionine [CPD:
C00019 ]
Product
4-demethylwyosine37 in tRNAPhe;
L-methionine [CPD:
C00073 ];
5'-deoxyadenosine [CPD:
C05198 ];
CO2 [CPD:
C00011 ];
H2O [CPD:
C00001 ]
Comment
This enzyme, which is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes, binds two [4Fe-4S] clusters [3,4]. Carbons C2 and C3 from pyruvate are incorporated into 4-demethylwyosine [3]. The enzyme is found in eukaryotes where it is part of the pathway for wybutosine synthesis, and in archaea, where it is involved in the biosynthesis of archaeal wye bases, such as wyosine, isowyosine, and methylwyosine.
History
EC 4.1.3.44 created 2013
Orthology
K15449 tRNA wybutosine-synthesizing protein 1
Genes
HSA : 441250(TYW1B) 55253(TYW1)
PTR : 472401(TYW1B) 744965
PPS : 100969148 117978806(TYW1B)
BTAX : 128070359 128071308
CDK : 105089694 116151342 116152013
MMEA : 130580248 130586624
SANH : 107659913 107659914 107672403
MANU : 129437833 129437834
PSPA : 121308574 121308578(tyw1)
ARUT : 117429105 117963254
LPIC : 129253662 129254981
DPTE : 113794424 113796780 113797569
RPHI : 132742714 132749430
CSAT : 104702257 104713164 104751391
BNA : 106353668 106354510 106406196
RSZ : 108814199 108818191 108831658 130507637
APRC : 113846615 113846891
AIP : 107631952 107631972 107647819
AHF : 112697963 112734880 112756272
MSYL : 126603484 126631717
PXB : 103928945 103942715 103954679 103955407
SSTN : 125842510 125854755
SSPL : 121753338 121766086
SMIL : 131009772 131010520
PSOM : 113287835 113288631
TAES : 123105194 123113472 123122993
MFLO : 136536097 136536102
PVIR : 120648981 120688642
CGR : 2887518(GVI51_E05401)
NCS : NCAS_0A01070(NCAS0A01070)
NDI : NDAI_0F01620(NDAI0F01620)
TPF : TPHA_0J02420(TPHA0J02420)
TBL : TBLA_0B05360(TBLA0B05360)
TDL : TDEL_0E05290(TDEL0E05290)
KAF : KAFR_0K00300(KAFR0K00300)
KNG : KNAG_0D01110(KNAG0D01110)
LBG : 92209343(LODBEIA_P41470)
CAL : CAALFM_C602290CA(CaO19.3470)
YLI : 2912065(YALI2_F00406g)
NTE : NEUTE1DRAFT59896(NEUTE1DRAFT_59896)
SMP : 10803976(SMAC4_04759)
TATV : 25785392(TrAtP1_001409)
TASP : 36614292(TrAFT101_001063)
PLJ : 28883012(PLICBS_000974)
CDET : 87941864(CDEST_05361)
BFU : BCIN_12g03860(Bctyw1)
CPW : 9694575(D8B26_002546)
PTRR : 6347330(PtrM4_035240)
PLAG : 39740554(PADL01_0523900)
PBRS : 92371235(MKS88_003148)
TGO : TGME49_272270 TGME49_315958
BLAC : 94352138(CCR75_008415)
TBR : Tb09.160.3520 Tb927.7.7130
TBG : TbgDal_IX2650 TbgDal_VII8390
LMA : LMJF_05_0750 LMJF_15_1540
LIF : LINJ_05_0750 LINJ_15_1610
LDO : LDBPK_050750 LDBPK_151610
LMI : LMXM_05_0750 LMXM_15_1540
LMAT : 92517623(LSCM1_07752)
LBZ : LBRM_05_0730 LBRM_15_1540
LPAN : LPMP_050730 LPMP_151500
LOI : 92363159(LSCM4_07330) 92363890(LSCM4_08080)
LEIS : 94183208(GH5_07988)
LENR : 94174801(CUR178_07650)
LEIN : 94190128(JIQ42_06520) 94191631(JIQ42_08063)
PHET : 94292215(JKF63_06188) 94293419(JKF63_07403)
EHX : EMIHUDRAFT_426304 EMIHUDRAFT_428437
GTT : GUITHDRAFT_52860 GUITHDRAFT_85567
MJK : N2V74_00145 N2V74_05705
TVO : TVG0493454(TVG0493454)
LOKI : Lokiarch_15360(taw1_1) Lokiarch_18480(taw1_2)
» show all
Taxonomy
Reference
Authors
Goto-Ito S, Ishii R, Ito T, Shibata R, Fusatomi E, Sekine SI, Bessho Y, Yokoyama S
Title
Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis.
Journal
Sequence
Reference
Authors
Suzuki Y, Noma A, Suzuki T, Senda M, Senda T, Ishitani R, Nureki O
Title
Crystal structure of the radical SAM enzyme catalyzing tricyclic modified base formation in tRNA.
Journal
Sequence
Reference
Authors
Young AP, Bandarian V
Title
Pyruvate is the source of the two carbons that are required for formation of the imidazoline ring of 4-demethylwyosine.
Journal
Reference
Authors
Perche-Letuvee P, Kathirvelu V, Berggren G, Clemancey M, Latour JM, Maurel V, Douki T, Armengaud J, Mulliez E, Fontecave M, Garcia-Serres R, Gambarelli S, Atta M
Title
4-Demethylwyosine synthase from Pyrococcus abyssi is a radical-S-adenosyl-L-methionine enzyme with an additional [4Fe-4S](+2) cluster that interacts with the pyruvate co-substrate.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 4.1.3.44
ExPASy - ENZYME nomenclature database: 4.1.3.44