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Protein

tRNA-5-methyluridine(54) 2-sulfurtransferase

Gene

ttuA

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m5s2U or s2T) (PubMed:28655838). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures (By similarity). Can use free sulfide as sulfur source in vitro, which may be also the sulfur source in vivo (PubMed:28655838).By similarity1 Publication

Miscellaneous

In TtuA from T.thermophilus, the sulfur inserted into the nucleoside comes from the C-terminal thiocarboxylate of TtuB, but there is no TtuB ortholog in P.horikoshii. Free sulfide has been shown to be present at relatively high concentrations within thermophilic archaea, and may be the sulfur source in vivo.Curated
The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster.1 Publication

Catalytic activityi

ATP + hydrogen sulfide + 5-methyluracil(54) in tRNA = AMP + diphosphate + 5-methyl-2-thiouracil(54) in tRNA.1 Publication

Cofactori

Protein has several cofactor binding sites:

Pathwayi: tRNA modification

This protein is involved in tRNA modification.1 Publication
View all proteins of this organism that are known to be involved in tRNA modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi3Zinc 1Combined sources2 Publications1
Metal bindingi6Zinc 1Combined sources2 Publications1
Metal bindingi22Zinc 1Combined sources2 Publications1
Metal bindingi25Zinc 1; via pros nitrogenCombined sources2 Publications1
Binding sitei53ATP; via carbonyl oxygen1 Publication1
Binding sitei79ATP; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi128Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi131Iron-sulfur (4Fe-4S)1 Publication1
Binding sitei135ATP1 Publication1
Binding sitei154ATP; via amide nitrogen1 Publication1
Metal bindingi220Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi272Zinc 2Combined sources2 Publications1
Metal bindingi275Zinc 2Combined sources2 Publications1
Metal bindingi284Zinc 2Combined sources2 Publications1
Metal bindingi287Zinc 2Combined sources2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRNA-binding, Transferase, tRNA-binding
Biological processtRNA processing
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-283-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-5-methyluridine(54) 2-sulfurtransferase1 Publication (EC:2.8.1.-1 Publication)
Alternative name(s):
tRNA thiouridine synthetase TtuA1 Publication
Gene namesi
Name:ttuA2 Publications
Ordered Locus Names:PH0300Imported
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59D → A: Loss of binding to ATP. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004423611 – 310tRNA-5-methyluridine(54) 2-sulfurtransferaseAdd BLAST310

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi128 ↔ 220AlternateCombined sources2 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi70601.PH0300.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VRHX-ray2.10A1-310[»]
5MKOX-ray2.65A/B1-310[»]
5MKPX-ray2.50A1-310[»]
5MKQX-ray2.79A/B1-310[»]
ProteinModelPortaliO58038.
SMRiO58038.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TtcA family. TtuA subfamily.Curated

Phylogenomic databases

eggNOGiarCOG00042. Archaea.
COG0037. LUCA.
HOGENOMiHOG000225863.
KOiK21947.
OMAiNKFAYDN.
OrthoDBiPOG093Z07BB.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiView protein in InterPro
IPR000541. Ncs6/Tuc1/Ctu1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. TilS/TtcA_N.
IPR035107. tRNA_thiolation_TtcA_Ctu1.
PfamiView protein in Pfam
PF01171. ATP_bind_3. 1 hit.
PIRSFiPIRSF004976. ATPase_YdaO. 1 hit.
TIGRFAMsiTIGR00269. TIGR00269. 1 hit.

Sequencei

Sequence statusi: Complete.

O58038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCKFCSREA YIKIHYPKMY LCEEHFKEYF ERKVSRTIER YKLLTKDERI
60 70 80 90 100
LVAVSGGKDS AVTAYVLKKL GYNIECLHIN LGISGYSEKS EEYAKKQCKL
110 120 130 140 150
IGAPLHIVRI KEILGYGIGE VKTRRPPCSY CGLTKRYIMN KFAYDNGFDA
160 170 180 190 200
IATGHNLDDE ASFLLNNILH WNTEYLAKGG PILPQQGKFI KKVKPLYEVT
210 220 230 240 250
EREVVAYALA VGLEYIVEEC PYARGATTLD MKGVLNELEE KRPGTKFNFV
260 270 280 290 300
RGYLKKKKLF EPEIKEKEIK ECKICRMPSS GDICAFCKFW GLKKEINFKV
310
SSTDEEPFGP
Length:310
Mass (Da):35,633
Last modified:August 1, 1998 - v1
Checksum:i87870CE4006C4246
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29373.1.
PIRiF71455.
RefSeqiWP_010884395.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29373; BAA29373; BAA29373.
GeneIDi1444182.
KEGGipho:PH0300.

Similar proteinsi

Entry informationi

Entry nameiTTUA_PYRHO
AccessioniPrimary (citable) accession number: O58038
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2017
Last sequence update: August 1, 1998
Last modified: November 22, 2017
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families