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P07649 (TRUA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA pseudouridine synthase A

EC=5.4.99.12
Alternative name(s):
tRNA pseudouridine(38-40) synthase
tRNA pseudouridylate synthase I
Short name=PSU-I
tRNA-uridine isomerase I
Gene names
Name:truA
Synonyms:asuC, hisT, leuK
Ordered Locus Names:b2318, JW2315
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. Ref.11

Catalytic activity

tRNA uridine(38-40) = tRNA pseudouridine(38-40). Ref.11

Subunit structure

Homodimer. Ref.10 Ref.11

Sequence similarities

Belongs to the tRNA pseudouridine synthase TruA family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270tRNA pseudouridine synthase A HAMAP-Rule MF_00171
PRO_0000057375

Regions

Region107 – 1115RNA binding HAMAP-Rule MF_00171
Region168 – 1725Interaction with tRNA HAMAP-Rule MF_00171

Sites

Active site601Nucleophile Ref.8 Ref.9
Binding site1181Substrate
Site581Interaction with tRNA; Important for base-flipping
Site781Interaction with tRNA
Site1101Interaction with tRNA
Site1261Interaction with tRNA
Site1391Interaction with tRNA

Experimental info

Mutagenesis581R → A: Loss of activity. Ref.11

Secondary structure

............................................... 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07649 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 8E97BC88C3220188

FASTA27030,400
        10         20         30         40         50         60 
MSDQQQPPVY KIALGIEYDG SKYYGWQRQN EVRSVQEKLE KALSQVANEP ITVFCAGRTD 

        70         80         90        100        110        120 
AGVHGTGQVV HFETTALRKD AAWTLGVNAN LPGDIAVRWV KTVPDDFHAR FSATARRYRY 

       130        140        150        160        170        180 
IIYNHRLRPA VLSKGVTHFY EPLDAERMHR AAQCLLGEND FTSFRAVQCQ SRTPWRNVMH 

       190        200        210        220        230        240 
INVTRHGPYV VVDIKANAFV HHMVRNIVGS LMEVGAHNQP ESWIAELLAA KDRTLAAATA 

       250        260        270 
KAEGLYLVAV DYPDRYDLPK PPMGPLFLAD 

« Hide

References

« Hide 'large scale' references
[1]"Structural features of the hisT operon of Escherichia coli K-12."
Arps P.J., Marvel C.C., Rubin B.C., Tolan D.A., Penhoet E.E., Winkler M.E.
Nucleic Acids Res. 13:5297-5315(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons."
Nonet M.L., Marvel C.C., Tolan D.R.
J. Biol. Chem. 262:12209-12217(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 255-270.
Strain: K12.
[6]"Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette."
Arps P.J., Winkler M.E.
J. Bacteriol. 169:1061-1070(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10 AND 267-270.
Strain: K12.
[7]"Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I."
Kammen H.O., Marvel C.C., Hardy L., Penhoet E.E.
J. Biol. Chem. 263:2255-2263(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, CHARACTERIZATION.
[8]"A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst."
Huang L., Pookanjanatavip M., Gu X., Santi D.V.
Biochemistry 37:344-351(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[9]"The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA."
Gu X., Liu Y., Santi D.V.
Proc. Natl. Acad. Sci. U.S.A. 96:14270-14275(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[10]"The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I."
Foster P.G., Huang L., Santi D.V., Stroud R.M.
Nat. Struct. Biol. 7:23-27(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 7-270, SUBUNIT.
[11]"How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA."
Hur S., Stroud R.M.
Mol. Cell 26:189-203(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 7-270 IN COMPLEX WITH TRNA, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-58.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02743 Genomic DNA. Translation: CAA26522.1.
U00096 Genomic DNA. Translation: AAC75378.1.
AP009048 Genomic DNA. Translation: BAA16175.1.
M68934 Genomic DNA. Translation: AAA23963.1.
M15542 Genomic DNA. Translation: AAA24313.1.
M15543 Genomic DNA. No translation available.
PIRSYECZ1. B23792.
RefSeqNP_416821.1. NC_000913.3.
YP_490560.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJ0X-ray1.50A/B7-270[»]
2NQPX-ray3.50A/B/C/D1-270[»]
2NR0X-ray3.90A/B/C/D1-270[»]
2NREX-ray4.00A1-270[»]
ProteinModelPortalP07649.
SMRP07649. Positions 7-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11043N.
IntActP07649. 9 interactions.
MINTMINT-1310146.
STRING511145.b2318.

Proteomic databases

PaxDbP07649.
PRIDEP07649.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75378; AAC75378; b2318.
BAA16175; BAA16175; BAA16175.
GeneID12932365.
946793.
KEGGecj:Y75_p2284.
eco:b2318.
PATRIC32120007. VBIEscCol129921_2413.

Organism-specific databases

EchoBASEEB0449.
EcoGeneEG10454. truA.

Phylogenomic databases

eggNOGCOG0101.
HOGENOMHOG000248672.
KOK06173.
OMAQANAFVH.
OrthoDBEOG6Z9B4R.
PhylomeDBP07649.

Enzyme and pathway databases

BioCycEcoCyc:EG10454-MONOMER.
ECOL316407:JW2315-MONOMER.
MetaCyc:EG10454-MONOMER.
BRENDA5.4.99.12. 2026.

Gene expression databases

GenevestigatorP07649.

Family and domain databases

Gene3D3.30.70.580. 1 hit.
3.30.70.660. 1 hit.
HAMAPMF_00171. TruA.
InterProIPR020103. PsdUridine_synth_cat_dom.
IPR001406. PsdUridine_synth_TruA.
IPR020097. PsdUridine_synth_TruA_a/b_dom.
IPR020095. PsdUridine_synth_TruA_C.
IPR020094. PsdUridine_synth_TruA_N.
[Graphical view]
PANTHERPTHR11142. PTHR11142. 1 hit.
PfamPF01416. PseudoU_synth_1. 2 hits.
[Graphical view]
PIRSFPIRSF001430. tRNA_psdUrid_synth. 1 hit.
SUPFAMSSF55120. SSF55120. 1 hit.
TIGRFAMsTIGR00071. hisT_truA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP07649.
PROP07649.

Entry information

Entry nameTRUA_ECOLI
AccessionPrimary (citable) accession number: P07649
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 14, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene