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Protein

tRNA pseudouridine synthase A

Gene

truA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.1 Publication

Catalytic activityi

tRNA uridine(38-40) = tRNA pseudouridine(38-40).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Interaction with tRNA; Important for base-flipping
Active sitei60 – 601Nucleophile2 Publications
Sitei78 – 781Interaction with tRNA
Sitei110 – 1101Interaction with tRNA
Binding sitei118 – 1181Substrate
Sitei126 – 1261Interaction with tRNA
Sitei139 – 1391Interaction with tRNA

GO - Molecular functioni

  • pseudouridine synthase activity Source: EcoCyc
  • tRNA binding Source: EcoCyc

GO - Biological processi

  • tRNA pseudouridine synthesis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciEcoCyc:EG10454-MONOMER.
ECOL316407:JW2315-MONOMER.
MetaCyc:EG10454-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:truA
Synonyms:asuC, hisT, leuK
Ordered Locus Names:b2318, JW2315
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10454. truA.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581R → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270tRNA pseudouridine synthase APRO_0000057375Add
BLAST

Proteomic databases

PaxDbiP07649.
PRIDEiP07649.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

DIPiDIP-11043N.
IntActiP07649. 9 interactions.
MINTiMINT-1310146.
STRINGi511145.b2318.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 189Combined sources
Helixi20 – 223Combined sources
Beta strandi30 – 323Combined sources
Helixi35 – 4713Combined sources
Beta strandi53 – 575Combined sources
Beta strandi64 – 7512Combined sources
Helixi80 – 8910Combined sources
Beta strandi95 – 1028Combined sources
Turni109 – 1124Combined sources
Beta strandi115 – 1239Combined sources
Beta strandi125 – 1273Combined sources
Turni131 – 1344Combined sources
Beta strandi135 – 1384Combined sources
Helixi145 – 1528Combined sources
Helixi153 – 1553Combined sources
Beta strandi157 – 1604Combined sources
Helixi162 – 1643Combined sources
Beta strandi175 – 18612Combined sources
Beta strandi189 – 1979Combined sources
Helixi203 – 21513Combined sources
Helixi223 – 2308Combined sources
Helixi233 – 2353Combined sources
Beta strandi245 – 2517Combined sources
Helixi254 – 2563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07649.
SMRiP07649. Positions 7-270.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07649.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1115RNA binding
Regioni168 – 1725Interaction with tRNA

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0101.
HOGENOMiHOG000248672.
InParanoidiP07649.
KOiK06173.
OMAiPWRNVHH.
OrthoDBiEOG6Z9B4R.
PhylomeDBiP07649.

Family and domain databases

Gene3Di3.30.70.580. 1 hit.
3.30.70.660. 1 hit.
HAMAPiMF_00171. TruA.
InterProiIPR020103. 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]
PANTHERiPTHR11142. PTHR11142. 1 hit.
PfamiPF01416. PseudoU_synth_1. 2 hits.
[Graphical view]
PIRSFiPIRSF001430. tRNA_psdUrid_synth. 1 hit.
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00071. hisT_truA. 1 hit.

Sequencei

Sequence statusi: Complete.

P07649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQQQPPVY KIALGIEYDG SKYYGWQRQN EVRSVQEKLE KALSQVANEP
60 70 80 90 100
ITVFCAGRTD AGVHGTGQVV HFETTALRKD AAWTLGVNAN LPGDIAVRWV
110 120 130 140 150
KTVPDDFHAR FSATARRYRY IIYNHRLRPA VLSKGVTHFY EPLDAERMHR
160 170 180 190 200
AAQCLLGEND FTSFRAVQCQ SRTPWRNVMH INVTRHGPYV VVDIKANAFV
210 220 230 240 250
HHMVRNIVGS LMEVGAHNQP ESWIAELLAA KDRTLAAATA KAEGLYLVAV
260 270
DYPDRYDLPK PPMGPLFLAD
Length:270
Mass (Da):30,400
Last modified:April 1, 1988 - v1
Checksum:i8E97BC88C3220188
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB23792. SYECZ1.
RefSeqiNP_416821.1. NC_000913.3.
WP_001283586.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75378; AAC75378; b2318.
BAA16175; BAA16175; BAA16175.
GeneIDi946793.
KEGGieco:b2318.
PATRICi32120007. VBIEscCol129921_2413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB23792. SYECZ1.
RefSeqiNP_416821.1. NC_000913.3.
WP_001283586.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07649.
SMRiP07649. Positions 7-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-11043N.
IntActiP07649. 9 interactions.
MINTiMINT-1310146.
STRINGi511145.b2318.

Proteomic databases

PaxDbiP07649.
PRIDEiP07649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75378; AAC75378; b2318.
BAA16175; BAA16175; BAA16175.
GeneIDi946793.
KEGGieco:b2318.
PATRICi32120007. VBIEscCol129921_2413.

Organism-specific databases

EchoBASEiEB0449.
EcoGeneiEG10454. truA.

Phylogenomic databases

eggNOGiCOG0101.
HOGENOMiHOG000248672.
InParanoidiP07649.
KOiK06173.
OMAiPWRNVHH.
OrthoDBiEOG6Z9B4R.
PhylomeDBiP07649.

Enzyme and pathway databases

BioCyciEcoCyc:EG10454-MONOMER.
ECOL316407:JW2315-MONOMER.
MetaCyc:EG10454-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07649.
PROiP07649.

Family and domain databases

Gene3Di3.30.70.580. 1 hit.
3.30.70.660. 1 hit.
HAMAPiMF_00171. TruA.
InterProiIPR020103. 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]
PANTHERiPTHR11142. PTHR11142. 1 hit.
PfamiPF01416. PseudoU_synth_1. 2 hits.
[Graphical view]
PIRSFiPIRSF001430. tRNA_psdUrid_synth. 1 hit.
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00071. hisT_truA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiTRUA_ECOLI
AccessioniPrimary (citable) accession number: P07649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 22, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.