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Protein

S-adenosylmethionine:tRNA ribosyltransferase-isomerase

Gene

queA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).

Catalytic activityi

S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine(34) in tRNA = L-methionine + adenine + epoxyqueuosine(34) in tRNA.1 Publication

Enzyme regulationi

Inhibited by S-adenosylhomocysteine, adenosylornithine and products.

Kineticsi

  1. KM=98 µM for S-adenosylmethionine1 Publication
  2. KM=1.9 µM for 7-(aminomethyl)-7-deazaguanosine1 Publication

    Pathwayi: tRNA-queuosine biosynthesis

    This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.
    View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

    GO - Molecular functioni

    GO - Biological processi

    • queuosine biosynthetic process Source: EcoCyc
    • tRNA wobble guanine modification Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Queuosine biosynthesis

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10812-MONOMER.
    ECOL316407:JW0395-MONOMER.
    MetaCyc:EG10812-MONOMER.
    SABIO-RKP0A7F9.
    UniPathwayiUPA00392.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine:tRNA ribosyltransferase-isomerase (EC:2.4.99.17)
    Alternative name(s):
    Queuosine biosynthesis protein QueA
    Gene namesi
    Name:queA
    Ordered Locus Names:b0405, JW0395
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10812. queA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356S-adenosylmethionine:tRNA ribosyltransferase-isomerasePRO_0000165400Add
    BLAST

    Proteomic databases

    PaxDbiP0A7F9.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi4262056. 10 interactions.
    DIPiDIP-47972N.
    IntActiP0A7F9. 5 interactions.
    STRINGi511145.b0405.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A7F9.
    SMRiP0A7F9. Positions 6-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the QueA family.Curated

    Phylogenomic databases

    eggNOGiENOG4105E2N. Bacteria.
    COG0809. LUCA.
    HOGENOMiHOG000004401.
    InParanoidiP0A7F9.
    KOiK07568.
    OMAiYGDAMFL.
    OrthoDBiEOG6X6RBB.
    PhylomeDBiP0A7F9.

    Family and domain databases

    HAMAPiMF_00113. QueA.
    InterProiIPR003699. QueA.
    [Graphical view]
    PfamiPF02547. Queuosine_synth. 1 hit.
    [Graphical view]
    SUPFAMiSSF111337. SSF111337. 1 hit.
    TIGRFAMsiTIGR00113. queA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A7F9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVTDFSFEL PESLIAHYPM PERSSCRLLS LDGPTGALTH GTFTDLLDKL
    60 70 80 90 100
    NPGDLLVFNN TRVIPARLFG RKASGGKIEV LVERMLDDKR ILAHIRASKA
    110 120 130 140 150
    PKPGAELLLG DDESINATMT ARHGALFEVE FNDERSVLDI LNSIGHMPLP
    160 170 180 190 200
    PYIDRPDEDA DRELYQTVYS EKPGAVAAPT AGLHFDEPLL EKLRAKGVEM
    210 220 230 240 250
    AFVTLHVGAG TFQPVRVDTI EDHIMHSEYA EVPQDVVDAV LAAKARGNRV
    260 270 280 290 300
    IAVGTTSVRS LESAAQAAKN DLIEPFFDDT QIFIYPGFQY KVVDALVTNF
    310 320 330 340 350
    HLPESTLIML VSAFAGYQHT MNAYKAAVEE KYRFFSYGDA MFITYNPQAI

    NERVGE
    Length:356
    Mass (Da):39,431
    Last modified:June 7, 2005 - v1
    Checksum:i47F7F0090812DCF3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M37702 Genomic DNA. Translation: AAA16114.1.
    U82664 Genomic DNA. Translation: AAB40161.1.
    U00096 Genomic DNA. Translation: AAC73508.1.
    AP009048 Genomic DNA. Translation: BAE76185.1.
    PIRiB38530.
    RefSeqiNP_414939.1. NC_000913.3.
    WP_001266503.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73508; AAC73508; b0405.
    BAE76185; BAE76185; BAE76185.
    GeneIDi944905.
    KEGGiecj:JW0395.
    eco:b0405.
    PATRICi32115959. VBIEscCol129921_0421.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M37702 Genomic DNA. Translation: AAA16114.1.
    U82664 Genomic DNA. Translation: AAB40161.1.
    U00096 Genomic DNA. Translation: AAC73508.1.
    AP009048 Genomic DNA. Translation: BAE76185.1.
    PIRiB38530.
    RefSeqiNP_414939.1. NC_000913.3.
    WP_001266503.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP0A7F9.
    SMRiP0A7F9. Positions 6-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262056. 10 interactions.
    DIPiDIP-47972N.
    IntActiP0A7F9. 5 interactions.
    STRINGi511145.b0405.

    Proteomic databases

    PaxDbiP0A7F9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73508; AAC73508; b0405.
    BAE76185; BAE76185; BAE76185.
    GeneIDi944905.
    KEGGiecj:JW0395.
    eco:b0405.
    PATRICi32115959. VBIEscCol129921_0421.

    Organism-specific databases

    EchoBASEiEB0805.
    EcoGeneiEG10812. queA.

    Phylogenomic databases

    eggNOGiENOG4105E2N. Bacteria.
    COG0809. LUCA.
    HOGENOMiHOG000004401.
    InParanoidiP0A7F9.
    KOiK07568.
    OMAiYGDAMFL.
    OrthoDBiEOG6X6RBB.
    PhylomeDBiP0A7F9.

    Enzyme and pathway databases

    UniPathwayiUPA00392.
    BioCyciEcoCyc:EG10812-MONOMER.
    ECOL316407:JW0395-MONOMER.
    MetaCyc:EG10812-MONOMER.
    SABIO-RKP0A7F9.

    Miscellaneous databases

    PROiP0A7F9.

    Family and domain databases

    HAMAPiMF_00113. QueA.
    InterProiIPR003699. QueA.
    [Graphical view]
    PfamiPF02547. Queuosine_synth. 1 hit.
    [Graphical view]
    SUPFAMiSSF111337. SSF111337. 1 hit.
    TIGRFAMsiTIGR00113. queA. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Structure and organization of Escherichia coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes."
      Reuter K., Slany R., Ullrich F., Kersten H.
      J. Bacteriol. 173:2256-2264(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine."
      Slany R.K., Boesl M., Crain P.F., Kersten H.
      Biochemistry 32:7811-7817(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "Transfer and isomerization of the ribose moiety of AdoMet during the biosynthesis of queuosine tRNAs, a new unique reaction catalyzed by the QueA protein from Escherichia coli."
      Slany R.K., Boesl M., Kersten H.
      Biochimie 76:389-393(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, REACTION MECHANISM.
      Strain: K12.
    7. "Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA)."
      Van Lanen S.G., Iwata-Reuyl D.
      Biochemistry 42:5312-5320(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITORS.
      Strain: K12 / DH5-alpha.

    Entry informationi

    Entry nameiQUEA_ECOLI
    AccessioniPrimary (citable) accession number: P0A7F9
    Secondary accession number(s): P21516, Q2MC21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: January 20, 2016
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This reaction follows a completely ordered sequential bi-ter kinetic mechanism, with binding of preQ1-tRNATyr followed by AdoMet to form the ternary complex. Products are then released in the following order: adenine, methionine, and oQ-tRNATyr.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    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 one 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.