KEGG   ENZYME: 2.8.1.15
Entry
EC 2.8.1.15                 Enzyme                                 

Name
tRNA-5-methyluridine54 2-sulfurtransferase;
TtuA
Class
Transferases;
Transferring sulfur-containing groups;
Sulfurtransferases
Sysname
[TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH:tRNA (5-methyluridine54-2-O)-sulfurtransferase
Reaction(IUBMB)
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyluracil54 in tRNA + H2O = AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly
Substrate
ATP [CPD:C00002];
[TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH;
5-methyluracil54 in tRNA;
H2O [CPD:C00001]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
5-methyl-2-thiouracil54 in tRNA;
[TtuB sulfur-carrier protein]-Gly-Gly
Comment
The enzyme, found in thermophilic bacteria and archaea, modifies the ribothymidine (5-methyluridine) residue at position 54 of tRNAs. Contains zinc and an [4Fe-4S] cluster. Some organisms, such as the archaeon Pyrococcus horikoshii, do not have a TtuB sulfur-carrier protein, and appear to use sulfide as the sulfur source.
History
EC 2.8.1.15 created 2017
Orthology
K21947  tRNA-5-methyluridine54 2-sulfurtransferase
Genes
DVU: DVU0135
DVL: Dvul_2830
DVM: DvMF_2330
DVG: Deval_0160
DDE: Dde_3611
DDS: Ddes_2277
DDN: DND132_1127
DMA: DMR_30620
DSA: Desal_1104
DHY: DESAM_21692
DGG: DGI_0441
DFL: DFE_1672
DAS: Daes_2444
DPI: BN4_10998
PPRF: DPRO_2984
DBA: Dbac_1482
DRT: Dret_1363
SFU: Sfum_0716
DBR: Deba_3267
DAU: Daud_1159
TMR: Tmar_2076
TTE: TTE0073(MesJ) TTE2470(MesJ4)
TIT: Thit_0462
ADG: Adeg_0170
TPZ: Tph_c13040(ttcA1)
CSC: Csac_0104
ATE: Athe_0195
TOC: Toce_1816
TACI: TDSAC_1197
MHAS: MHAS_03206(ttcA)
TTH: TT_C0106
TTJ: TTHA0477
TAQ: TO73_1857
TLI: Tlie_1905
AAE: aq_1333
TAL: Thal_0032
TMA: TM0197
TMW: THMA_0204
TMQ: THMB_0204
TMX: THMC_0204
TPT: Tpet_0727
TRQ: TRQ2_0751
TNA: CTN_0489
TNP: Tnap_0827
TLE: Tlet_0417
TME: Tmel_1006
TAF: THA_1285
THER: Y592_05865
FNO: Fnod_1006
KOL: Kole_1722
CEX: CSE_02580
DTU: Dtur_1672
NDE: NIDE3396
NJA: NSJP_0222
LFC: LFE_0457
CTHI: THC_0836
MJA: MJ_1478
MFV: Mfer_1176
MKA: MK0144
AFU: AF_1321
FPL: Ferp_1084
GAC: GACE_0225
GAH: GAH_00072
ABI: Aboo_0768
PFU: PF0273
PFI: PFC_00430
PHO: PH0300(PH0300)
PAB: PAB1092
PYN: PNA2_0919
PYS: Py04_0428
TKO: TK1556
TON: TON_1717
TGA: TGAM_2130
TSI: TSIB_0454
THE: GQS_06720
THA: TAM4_293
THM: CL1_0970
TLT: OCC_10073
THS: TES1_1901
TNU: BD01_1355
TEU: TEU_02835
PPAC: PAP_01580
APE: APE_2086
ACJ: ACAM_1305
IHO: Igni_0707
IIS: EYM_07570
IAG: Igag_0555
STO: STK_06300
SAI: Saci_0378
MSE: Msed_1487
MCN: Mcup_0774
AHO: Ahos_0949
STEP: IC006_1661
PIS: Pisl_0017
PCL: Pcal_2018
POG: Pogu_1236
VDI: Vdis_2265
ASC: ASAC_0917
KCR: Kcr_0210
 » show all
Reference
1  [PMID:16547008]
  Authors
Shigi N, Sakaguchi Y, Suzuki T, Watanabe K
  Title
Identification of two tRNA thiolation genes required for cell growth at extremely high temperatures.
  Journal
J Biol Chem 281:14296-306 (2006)
DOI:10.1074/jbc.M511675200
  Sequence
[tth:TT_C0106]
Reference
2  [PMID:16317006]
  Authors
Shigi N, Suzuki T, Terada T, Shirouzu M, Yokoyama S, Watanabe K
  Title
Temperature-dependent biosynthesis of 2-thioribothymidine of Thermus thermophilus tRNA.
  Journal
J Biol Chem 281:2104-13 (2006)
DOI:10.1074/jbc.M510771200
Reference
3  [PMID:23444054]
  Authors
Nakagawa H, Kuratani M, Goto-Ito S, Ito T, Katsura K, Terada T, Shirouzu M, Sekine S, Shigi N, Yokoyama S
  Title
Crystallographic and mutational studies on the tRNA thiouridine synthetase TtuA.
  Journal
Proteins 81:1232-44 (2013)
DOI:10.1002/prot.24273
  Sequence
[pho:PH0300]
Reference
4  [PMID:27710943]
  Authors
Chen M, Narai S, Omura N, Shigi N, Chimnaronk S, Tanaka Y, Yao M
  Title
Crystallographic study of the 2-thioribothymidine-synthetic complex TtuA-TtuB from Thermus thermophilus.
  Journal
Acta Crystallogr F Struct Biol Commun 72:777-781 (2016)
DOI:10.1107/S2053230X16014242
  Sequence
[tth:TT_C0106]
Other DBs
ExplorEnz - The Enzyme Database: 2.8.1.15
IUBMB Enzyme Nomenclature: 2.8.1.15
ExPASy - ENZYME nomenclature database: 2.8.1.15
BRENDA, the Enzyme Database: 2.8.1.15

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