KEGG   ENZYME: 2.7.7.79Help
Entry
EC 2.7.7.79                 Enzyme                                 

Name
tRNAHis guanylyltransferase;
histidine tRNA guanylyltransferase;
Thg1p (ambiguous);
Thg1 (ambiguous)
Class
Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
BRITE hierarchy
Sysname
p-tRNAHis:GTP guanylyltransferase (ATP-hydrolysing)
Reaction(IUBMB)
p-tRNAHis + ATP + GTP = pppGp-tRNAHis + AMP + diphosphate (overall reaction);
(1a) p-tRNAHis + ATP = App-tRNAHis + diphosphate;
(1b) App-tRNAHis + GTP = pppGp-tRNAHis + AMP
Substrate
p-tRNAHis;
ATP [CPD:C00002];
GTP [CPD:C00044];
App-tRNAHis
Product
pppGp-tRNAHis;
AMP [CPD:C00020];
diphosphate [CPD:C00013];
App-tRNAHis
Comment
In eukarya an additional guanosine residue is added post-transcriptionally to the 5'-end of tRNAHis molecules. The addition occurs opposite a universally conserved adenosine73 and is thus the result of a non-templated 3'-5' addition reaction. The additional guanosine residue is an important determinant for aminoacylation by EC 6.1.1.21, histidyl-tRNA ligase.
The enzyme requires a divalent cation for activity [2]. ATP activation is not required when the substrate contains a 5'-triphosphate (ppp-tRNAHis) [3].
History
EC 2.7.7.79 created 2011
Orthology
K10761  
tRNA(His) guanylyltransferase
Genes
HSA: 
54974(THG1L)
PTR: 
462226(THG1L)
PPS: 
100985901(THG1L)
GGO: 
101136725(THG1L)
PON: 
100433264(THG1L)
MCC: 
715853(THG1L)
MCF: 
102115652(THG1L)
MMU: 
66628(Thg1l)
RNO: 
303067(Thg1l)
CGE: 
100763395(Thg1l)
HGL: 
101705954(Thg1l)
TUP: 
102469988(THG1L)
CFA: 
479315(THG1L)
AML: 
FCA: 
101080614(THG1L)
PTG: 
102957279(THG1L)
BTA: 
507084(THG1L)
BOM: 
102269225(THG1L)
PHD: 
102314984(THG1L)
CHX: 
102177794(THG1L)
OAS: 
101113674(THG1L)
SSC: 
100521164(THG1L)
CFR: 
102513875(THG1L)
BACU: 
103012052(THG1L)
LVE: 
103089991(THG1L)
ECB: 
100071194(THG1L)
MYB: 
102250438(THG1L)
MYD: 
102771832(THG1L)
PALE: 
102882192(THG1L)
MDO: 
100025355(THG1L)
SHR: 
100928502(THG1L)
OAA: 
100075219(THG1L)
GGA: 
416242(THG1L)
MGP: 
TGU: 
100223262(THG1L)
FAB: 
101806182(THG1L)
PHI: 
102104035(THG1L)
APLA: 
101790653(THG1L)
FPG: 
101915135(THG1L)
FCH: 
102051978(THG1L)
CLV: 
102088249(THG1L)
ASN: 
102385703(THG1L)
AMJ: 
102571463(THG1L)
PSS: 
102459768(THG1L)
CMY: 
102941033(THG1L)
ACS: 
100567729(thg1l)
PBI: 
XLA: 
495483(thg1l)
XTR: 
DRE: 
492814(thg1l)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102352205(THG1L)
CMK: 
103177299(thg1l)
BFO: 
CIN: 
SPU: 
DME: 
Dmel_CG4103(l(2)35Bc)
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
POPTR_0002s23440g(POPTRDRAFT_409100)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os05t0535500-01(Os05g0535500)
OBR: 
BDI: 
SBI: 
SORBI_09g026710(SORBIDRAFT_09g026710)
SITA: 
ATR: 
s00104p00090580(AMTR_s00104p00090580)
SMO: 
PPP: 
CRE: 
VCN: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
YGR024C(THG1)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NDI: 
NDAI_0D03900(NDAI0D03900)
TPF: 
TPHA_0F00940(TPHA0F00940)
TBL: 
TBLA_0G01180(TBLA0G01180)
TDL: 
TDEL_0D02910(TDEL0D02910)
KAF: 
KAFR_0F03760(KAFR0F03760)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CaO19.7063(THG1) CaO19_7063(CaJ7_0070)
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
AFM: 
AOR: 
AOR_1_852154(AO090003000484)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
PNO: 
PTE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
PPL: 
DSQ: 
SHS: 
PCO: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT121643(AGABI1DRAFT_121643)
ABV: 
AGABI2DRAFT200849(AGABI2DRAFT_200849)
CPUT: 
SLA: 
UMA: 
PFP: 
MGL: 
PGR: 
MLR: 
WSE: 
MBR: 
DDI: 
DPP: 
DFA: 
PFA: 
PFD: 
PFH: 
PYO: 
PCB: 
PBE: 
PKN: 
PVX: 
PCY: 
TAN: 
TPV: 
BBO: 
BBOV_IV004960(23.m05909)
BEQ: 
CPV: 
TET: 
PTM: 
TVA: 
 » show all
Taxonomy
Reference
1  [PMID:1660462]
  Authors
Jahn D, Pande S
  Title
Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism.
  Journal
J. Biol. Chem. 266 (1991) 22832-6.
Reference
2  [PMID:1660461]
  Authors
Pande S, Jahn D, Soll D
  Title
Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties.
  Journal
J. Biol. Chem. 266 (1991) 22826-31.
Reference
3  [PMID:14633974]
  Authors
Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM
  Title
tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis.
  Journal
Genes. Dev. 17 (2003) 2889-901.
  Sequence
[sce:YGR024C]
Reference
4  [PMID:20660484]
  Authors
Placido A, Sieber F, Gobert A, Gallerani R, Giege P, Marechal-Drouard L
  Title
Plant mitochondria use two pathways for the biogenesis of tRNAHis.
  Journal
Nucleic. Acids. Res. 38 (2010) 7711-7.
  Sequence
Reference
5  [PMID:18366186]
  Authors
Jackman JE, Phizicky EM
  Title
Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase.
  Journal
Biochemistry. 47 (2008) 4817-25.
Reference
6  [PMID:21059936]
  Authors
Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublie S
  Title
tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 107 (2010) 20305-10.
  Sequence
[hsa:54974]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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