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P07649

- TRUA_ECOLI

UniProt

P07649 - TRUA_ECOLI

Protein

tRNA pseudouridine synthase A

Gene

truA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    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

    1. pseudouridine synthase activity Source: EcoCyc
    2. tRNA binding Source: EcoCyc

    GO - Biological processi

    1. tRNA pseudouridine synthesis Source: EcoCyc

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    tRNA processing

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10454-MONOMER.
    ECOL316407:JW2315-MONOMER.
    MetaCyc:EG10454-MONOMER.
    BRENDAi5.4.99.12. 2026.

    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: Chromosome, UP000000625: 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.

    Expressioni

    Gene expression databases

    GenevestigatoriP07649.

    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 – 189
    Helixi20 – 223
    Beta strandi30 – 323
    Helixi35 – 4713
    Beta strandi53 – 575
    Beta strandi64 – 7512
    Helixi80 – 8910
    Beta strandi95 – 1028
    Turni109 – 1124
    Beta strandi115 – 1239
    Beta strandi125 – 1273
    Turni131 – 1344
    Beta strandi135 – 1384
    Helixi145 – 1528
    Helixi153 – 1553
    Beta strandi157 – 1604
    Helixi162 – 1643
    Beta strandi175 – 18612
    Beta strandi189 – 1979
    Helixi203 – 21513
    Helixi223 – 2308
    Helixi233 – 2353
    Beta strandi245 – 2517
    Helixi254 – 2563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK06173.
    OMAiQANAFVH.
    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

    MSDQQQPPVY KIALGIEYDG SKYYGWQRQN EVRSVQEKLE KALSQVANEP    50
    ITVFCAGRTD AGVHGTGQVV HFETTALRKD AAWTLGVNAN LPGDIAVRWV 100
    KTVPDDFHAR FSATARRYRY IIYNHRLRPA VLSKGVTHFY EPLDAERMHR 150
    AAQCLLGEND FTSFRAVQCQ SRTPWRNVMH INVTRHGPYV VVDIKANAFV 200
    HHMVRNIVGS LMEVGAHNQP ESWIAELLAA KDRTLAAATA KAEGLYLVAV 250
    DYPDRYDLPK PPMGPLFLAD 270
    Length:270
    Mass (Da):30,400
    Last modified:April 1, 1988 - v1
    Checksum:i8E97BC88C3220188
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490560.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75378; AAC75378; b2318.
    BAA16175; BAA16175; BAA16175.
    GeneIDi12932365.
    946793.
    KEGGiecj:Y75_p2284.
    eco:b2318.
    PATRICi32120007. VBIEscCol129921_2413.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi B23792. SYECZ1.
    RefSeqi NP_416821.1. NC_000913.3.
    YP_490560.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DJ0 X-ray 1.50 A/B 7-270 [» ]
    2NQP X-ray 3.50 A/B/C/D 1-270 [» ]
    2NR0 X-ray 3.90 A/B/C/D 1-270 [» ]
    2NRE X-ray 4.00 A 1-270 [» ]
    ProteinModelPortali P07649.
    SMRi P07649. Positions 7-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11043N.
    IntActi P07649. 9 interactions.
    MINTi MINT-1310146.
    STRINGi 511145.b2318.

    Proteomic databases

    PaxDbi P07649.
    PRIDEi P07649.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75378 ; AAC75378 ; b2318 .
    BAA16175 ; BAA16175 ; BAA16175 .
    GeneIDi 12932365.
    946793.
    KEGGi ecj:Y75_p2284.
    eco:b2318.
    PATRICi 32120007. VBIEscCol129921_2413.

    Organism-specific databases

    EchoBASEi EB0449.
    EcoGenei EG10454. truA.

    Phylogenomic databases

    eggNOGi COG0101.
    HOGENOMi HOG000248672.
    KOi K06173.
    OMAi QANAFVH.
    OrthoDBi EOG6Z9B4R.
    PhylomeDBi P07649.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10454-MONOMER.
    ECOL316407:JW2315-MONOMER.
    MetaCyc:EG10454-MONOMER.
    BRENDAi 5.4.99.12. 2026.

    Miscellaneous databases

    EvolutionaryTracei P07649.
    PROi P07649.

    Gene expression databases

    Genevestigatori P07649.

    Family and domain databases

    Gene3Di 3.30.70.580. 1 hit.
    3.30.70.660. 1 hit.
    HAMAPi MF_00171. TruA.
    InterProi IPR020103. 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 ]
    PANTHERi PTHR11142. PTHR11142. 1 hit.
    Pfami PF01416. PseudoU_synth_1. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF001430. tRNA_psdUrid_synth. 1 hit.
    SUPFAMi SSF55120. SSF55120. 1 hit.
    TIGRFAMsi TIGR00071. hisT_truA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 135 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