tRNA sulfurtransferase (P77718)

Identification
Name:tRNA sulfurtransferase
Synonyms:
  • Sulfur carrier protein ThiS sulfurtransferase
  • Thiamine biosynthesis protein thiI
  • tRNA 4-thiouridine synthase
Gene Name:thiI
Enzyme Class:
Biological Properties
General Function:Involved in RNA binding
Specific Function:Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by iscS
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0[Enzyme]-S-sulfanylcysteine+1.0C15813 ↔ 1.0C15814
1.0[Enzyme]-S-sulfanylcysteine + 1.0C15813 ↔ 1.0C15814
ReactionCard
1.0Thumb+1.0'Activated' tRNA ↔ 1.0Thumb+1.0tRNA containing a thionucleotide
1.0L-Cysteine + 1.0'Activated' tRNA ↔ 1.0L-Serine + 1.0tRNA containing a thionucleotide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0IscS with bound sulfur+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb+1.0IscS sulfur acceptor protein+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Dehydroglycine + 1.01-Deoxy-D-xylulose 5-phosphate + 1.0Hydrogen ion + 1.0IscS with bound sulfur + 1.0NADPH → 1.04-Methyl-5-(2-phosphoethyl)-thiazole + 1.0Adenosine monophosphate + 1.0Carbon dioxide + 2.0Water + 1.0IscS sulfur acceptor protein + 1.0NADP + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0'activated' tRNA → 1.0Thumb+1.0tRNA containing a thionucleotide
1.0L-Cysteine + 1.0'activated' tRNA → 1.0L-Serine + 1.0tRNA containing a thionucleotide
ReactionCard
1.0[IscS]-SSH+1.0[ThiS]-COAMP → 1.0[IscS]-SH+1.0[ThiS]-COSH+1.0Thumb
1.0[IscS]-SSH + 1.0[ThiS]-COAMP → 1.0[IscS]-SH + 1.0[ThiS]-COSH + 1.0Adenosine monophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB012131-Deoxy-D-xylulose 5-phosphateMetaboCard
ECMDB200944-Methyl-5-(2-phosphoethyl)-thiazoleMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21328DehydroglycineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB00187L-SerineMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
nucleic acid binding
RNA binding
Process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
thiamin and derivative metabolic process
thiamin biosynthetic process
thiamin metabolic process
Gene Properties
Blattner:b0423
Gene OrientationClockwise
Centisome Percentage:9.50
Left Sequence End440773
Right Sequence End442221
Gene Sequence:
>1449 bp
ATGAAGTTTATCATTAAATTGTTCCCGGAAATCACCATCAAAAGCCAATCTGTGCGCTTG
CGCTTTATAAAAATCCTTACCGGGAACATTCGTAACGTTTTAAAGCACTATGATGAGACG
CTCGCTGTCGTCCGCCACTGGGATAACATCGAAGTTCGCGCAAAAGATGAAAACCAGCGT
CTGGCTATTCGCGACGCTCTGACCCGTATTCCGGGTATCCACCATATTCTCGAAGTCGAA
GACGTGCCGTTTACCGACATGCACGATATTTTCGAGAAAGCGTTGGTTCAGTATCGCGAT
CAGCTGGAAGGCAAAACCTTCTGCGTACGCGTGAAGCGCCGTGGCAAACATGATTTTAGC
TCGATTGATGTGGAACGTTACGTCGGCGGCGGTTTAAATCAGCATATTGAATCCGCGCGC
GTGAAGCTGACCAATCCGGATGTGACTGTCCATCTGGAAGTGGAAGACGATCGTCTCCTG
CTGATTAAAGGCCGCTACGAAGGTATTGGCGGTTTCCCGATCGGCACCCAGGAAGATGTG
CTGTCGCTCATTTCCGGTGGTTTCGACTCCGGTGTTTCCAGTTATATGTTGATGCGTCGC
GGCTGCCGCGTGCATTACTGCTTCTTTAACCTCGGCGGCGCGGCGCATGAAATTGGCGTG
CGTCAGGTGGCGCATTATCTGTGGAACCGCTTTGGCAGCTCCCACCGCGTGCGTTTTGTC
GCTATTAATTTCGAACCGGTCGTCGGGGAAATTCTCGAGAAAATCGACGACGGTCAGATG
GGCGTTATCCTCAAACGTATGATGGTGCGTGCCGCATCTAAAGTGGCTGAACGTTACGGC
GTACAGGCGCTGGTCACCGGCGAAGCGCTCGGCCAGGTGTCCAGCCAGACGCTGACCAAC
CTGCGCCTGATTGATAACGTCTCCGACACGCTGATCCTGCGTCCGCTGATCTCTTACGAC
AAAGAGCACATCATCAACCTGGCCCGCCAGATTGGCACCGAAGACTTTGCTCGCACGATG
CCGGAATATTGTGGTGTGATCTCCAAAAGCCCGACGGTGAAAGCAGTTAAATCGAAGATT
GAAGCGGAAGAAGAGAAGTTCGACTTCAGCATTCTCGATAAAGTGGTTGAGGAAGCGAAT
AACGTTGATATCCGCGAAATCGCCCAGCAGACCGAGCAGGAAGTGGTGGAAGTGGAAACC
GTCAATGGCTTCGGCCCGAACGACGTGATCCTCGATATCCGTTCTATCGATGAACAGGAA
GATAAGCCACTGAAAGTCGAAGGGATTGATGTGGTTTCTCTGCCGTTCTATAAACTGAGC
ACCAAATTTGGCGATCTCGACCAGAACAAAACCTGGCTGCTGTGGTGTGAGCGCGGGGTG
ATGAGCCGTCTGCAGGCGCTCTATCTGCGCGAGCAGGGCTTTAACAATGTGAAGGTATAT
CGCCCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:482
Protein Molecular Weight:54973
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>tRNA sulfurtransferase
MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQR
LAIRDALTRIPGIHHILEVEDVPFTDMHDIFEKALVQYRDQLEGKTFCVRVKRRGKHDFS
SIDVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLLIKGRYEGIGGFPIGTQEDV
LSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFV
AINFEPVVGEILEKIDDGQMGVILKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTN
LRLIDNVSDTLILRPLISYDKEHIINLARQIGTEDFARTMPEYCGVISKSPTVKAVKSKI
EAEEEKFDFSILDKVVEEANNVDIREIAQQTEQEVVEVETVNGFGPNDVILDIRSIDEQE
DKPLKVEGIDVVSLPFYKLSTKFGDLDQNKTWLLWCERGVMSRLQALYLREQGFNNVKVY
RP
References
External Links:
ResourceLink
Uniprot ID:P77718
Uniprot Name:THII_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674563
Ecogene ID:EG13273
Ecocyc:EG13273
ColiBase:b0423
Kegg Gene:b0423
EchoBASE ID:EB3058
CCDB:THII_ECOLI
BacMap:16128408
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kambampati, R., Lauhon, C. T. (2000). "Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA." J Biol Chem 275:10727-10730. Pubmed: 10753862
  • Mueller, E. G., Buck, C. J., Palenchar, P. M., Barnhart, L. E., Paulson, J. L. (1998). "Identification of a gene involved in the generation of 4-thiouridine in tRNA." Nucleic Acids Res 26:2606-2610. Pubmed: 9592144
  • Mueller, E. G., Palenchar, P. M. (1999). "Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis." Protein Sci 8:2424-2427. Pubmed: 10595545
  • Mueller, E. G., Palenchar, P. M., Buck, C. J. (2001). "The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA." J Biol Chem 276:33588-33595. Pubmed: 11443125
  • Palenchar, P. M., Buck, C. J., Cheng, H., Larson, T. J., Mueller, E. G. (2000). "Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate." J Biol Chem 275:8283-8286. Pubmed: 10722656
  • Taylor, S. V., Kelleher, N. L., Kinsland, C., Chiu, H. J., Costello, C. A., Backstrom, A. D., McLafferty, F. W., Begley, T. P. (1998). "Thiamin biosynthesis in Escherichia coli. Identification of ThiS thiocarboxylate as the immediate sulfur donor in the thiazole formation." J Biol Chem 273:16555-16560. Pubmed: 9632726
  • Wright, C. M., Christman, G. D., Snellinger, A. M., Johnston, M. V., Mueller, E. G. (2006). "Direct evidence for enzyme persulfide and disulfide intermediates during 4-thiouridine biosynthesis." Chem Commun (Camb) :3104-3106. Pubmed: 16855700
  • Wright, C. M., Palenchar, P. M., Mueller, E. G. (2002). "A paradigm for biological sulfur transfers via persulfide groups: a persulfide-disulfide-thiol cycle in 4-thiouridine biosynthesis." Chem Commun (Camb) :2708-2709. Pubmed: 12510310
  • You, D., Xu, T., Yao, F., Zhou, X., Deng, Z. (2008). "Direct evidence that ThiI is an ATP pyrophosphatase for the adenylation of uridine in 4-thiouridine biosynthesis." Chembiochem 9:1879-1882. Pubmed: 18604845