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)
NLE: 100602201(THG1L)
MCC: 715853(THG1L)
MCF: 102115652(THG1L)
CSAB: 103244877(THG1L)
RRO: 104662395(THG1L)
RBB: 108518389(THG1L)
CJC: 100392376(THG1L)
SBQ: 101054088(THG1L)
MMU: 66628(Thg1l)
RNO: 303067(Thg1l)
CGE: 100763395(Thg1l)
NGI: 103745469(Thg1l)
HGL: 101705954(Thg1l)
CCAN: 109696233(Thg1l)
OCU: 100353509(THG1L)
TUP: 102469988(THG1L)
CFA: 479315(THG1L)
AML: 100476440(THG1L)
UMR: 103664539(THG1L)
ORO: 101376826(THG1L)
FCA: 101080614(THG1L)
PTG: 102957279(THG1L)
AJU: 106967626(THG1L)
BTA: 507084(THG1L)
BOM: 102269225(THG1L)
BIU: 109562254(THG1L)
PHD: 102314984(THG1L)
CHX: 102177794(THG1L)
OAS: 101113674(THG1L)
SSC: 100521164(THG1L)
CFR: 102513875(THG1L)
CDK: 105095137(THG1L)
BACU: 103012052(THG1L)
LVE: 103089991(THG1L)
OOR: 101281191(THG1L)
ECB: 100071194(THG1L)
EPZ: 103547696(THG1L)
EAI: 106832134(THG1L)
MYB: 102250438(THG1L)
MYD: 102771832(THG1L)
HAI: 109388889(THG1L)
RSS: 109451855(THG1L)
PALE: 102882192(THG1L)
LAV: 100656079(THG1L)
TMU: 101346108
MDO: 100025355(THG1L)
SHR: 100928502(THG1L)
OAA: 100075219(THG1L)
GGA: 416242(THG1L)
MGP: 100541621(THG1L)
CJO: 107320397(THG1L)
APLA: 101790653(THG1L)
ACYG: 106032687(THG1L)
TGU: 100223262(THG1L)
GFR: 102037256(THG1L)
FAB: 101806182(THG1L)
PHI: 102104035(THG1L)
PMAJ: 107210915(THG1L)
CCW: 104689676(THG1L)
FPG: 101915135(THG1L)
FCH: 102051978(THG1L)
CLV: 102088249(THG1L)
EGZ: 104122569(THG1L)
AAM: 106493653(THG1L)
ASN: 102385703(THG1L)
AMJ: 102571463(THG1L)
PSS: 102459768(THG1L)
CMY: 102941033(THG1L)
CPIC: 101950893(THG1L)
ACS: 100567729(thg1l)
PVT: 110077850(THG1L)
PBI: 103056892(THG1L) 103064657
GJA: 107115677(THG1L)
XLA: 495483(thg1l.L)
XTR: 100487878(thg1l) 101733043
NPR: 108786333(THG1L)
DRE: 492814(thg1l)
SANH: 107680932(thg1l)
IPU: 108274462(thg1l)
AMEX: 103044514(thg1l)
TRU: 101073616(thg1l)
LCO: 104924232(thg1l)
NCC: 104946880(thg1l)
MZE: 101485778(thg1l)
OLA: 101162300(thg1l)
XMA: 102225768(thg1l)
PRET: 103470877(thg1l)
NFU: 107396285(thg1l)
CSEM: 103391403(thg1l)
LCF: 108882804(thg1l)
HCQ: 109524369(thg1l)
BPEC: 110162409(thg1l)
SASA: 100195605(thg1) 106604278
ELS: 105024422(thg1l)
SFM: 108936756(thg1l)
LCM: 102352205(THG1L)
CMK: 103177299(thg1l)
CIN: 100179812
SPU: 587315
APLC: 110977035
SKO: 100374565
DME: Dmel_CG4103(THG)
DSI: Dsimw501_GD21976(Dsim_GD21976)
MDE: 101889710
AAG: 5579197
AME: 410055
BIM: 100741551
BTER: 100651919
SOC: 105206596
AEC: 105147260
ACEP: 105625037
PBAR: 105426638
HST: 105182218
CFO: 105248169
LHU: 105673503
PGC: 109856660
NVI: 100117826
TCA: 663767
DPA: 109539731
NVL: 108558615
BMOR: 692885
PMAC: 106719786
PRAP: 110999638
PXY: 105387318
API: 100165160
DNX: 107174143
ZNE: 110836441
TUT: 107368606
CRG: 105317995
MYI: 110452037
OBI: 106880761
LAK: 106164463
SHX: MS3_03130
EGL: EGR_02605
EPA: 110238492
ADF: 107345634
HMG: 100205492
AQU: 100636648
THJ: 104800903
CPAP: 110820238
CIT: 102626328
TCC: 18597151
GRA: 105768445
DZI: 111275196
EGR: 104415843
VRA: 106770861
CCAJ: 109789604
CAM: 101503826
LJA: Lj5g3v0523190.1(Lj5g3v0523190.1) Lj5g3v0523190.2(Lj5g3v0523190.2) Lj6g3v0291920.1(Lj6g3v0291920.1)
ADU: 107457887
AIP: 107608738
PPER: 18793967
PMUM: 103318902
CSV: 101208636
CMO: 103484683
MCHA: 111005370
CMAX: 111478015
CMOS: 111453416
CPEP: 111804307
RCU: 8264047
JCU: 105636568
POP: 7466188
JRE: 109005357
VVI: 100264494
SLY: 101259833
SPEN: 107017998
CANN: 107840624
NTO: 104086625
SIND: 105178315
HAN: 110886359
LSV: 111881383
DCR: 108197562
SOE: 110803554
NNU: 104605504
OSA: 4339440
DOSA: Os05t0535500-01(Os05g0535500)
OBR: 102722215
ATS: 109736984(LOC109736984) 109738565(LOC109738565)
SBI: 8068980
ZMA: 103630654
SITA: 101774960
PDA: 103706302
EGU: 105045590
MUS: 103993905
DCT: 110116034
AOF: 109820342
ATR: 18428407
PPP: 112284865
CRE: CHLREDRAFT_113708(THG1)
MNG: MNEG_7545
APRO: F751_0510
SCE: YGR024C(THG1)
ERC: Ecym_2419
KMX: KLMA_50212(THG1)
NDI: NDAI_0D03900(NDAI0D03900)
TPF: TPHA_0F00940(TPHA0F00940)
TBL: TBLA_0G01180(TBLA0G01180)
TDL: TDEL_0D02910(TDEL0D02910)
KAF: KAFR_0F03760(KAFR0F03760)
CAL: CAALFM_C700560CA(THG1)
CAUR: QG37_02648
SLB: AWJ20_712(THG1)
NCR: NCU02105
NTE: NEUTE1DRAFT70540(NEUTE1DRAFT_70540)
MGR: MGG_14742
SSCK: SPSK_05320
MAW: MAC_07406
MAJ: MAA_00661
CMT: CCM_05483
BFU: BCIN_05g04330(Bcthg1)
MBE: MBM_03855
ANI: AN0804.2
ANG: ANI_1_3196014(An01g12630)
CIM: CIMG_13693(CIMG03241)
PTE: PTT_11482
SPO: SPCC63.07
CNE: CNC02800
CNB: CNBC4410
ABP: AGABI1DRAFT121643(AGABI1DRAFT_121643)
ABV: AGABI2DRAFT200849(AGABI2DRAFT_200849)
MGL: MGL_1763
DDI: DDB_G0291830(thg1)
DFA: DFA_04027(thg1) DFA_05639
PCB: PCHAS_062220(PC301576.00.0)
TAN: TA19625
TPV: TP01_0248
BBO: BBOV_IV004960(23.m05909)
CPV: cgd1_1990
 » 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 266:22832-6 (1991)
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 266:22826-31 (1991)
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 17:2889-901 (2003)
DOI:10.1101/gad.1148603
  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 38:7711-7 (2010)
DOI:10.1093/nar/gkq646
  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 47:4817-25 (2008)
DOI:10.1021/bi702517q
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 107:20305-10 (2010)
DOI:10.1073/pnas.1010436107
  Sequence
[hsa:54974]
Other DBs
ExplorEnz - The Enzyme Database: 2.7.7.79
IUBMB Enzyme Nomenclature: 2.7.7.79
ExPASy - ENZYME nomenclature database: 2.7.7.79
BRENDA, the Enzyme Database: 2.7.7.79

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