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Q5X2V4

- HEM1_LEGPA

UniProt

Q5X2V4 - HEM1_LEGPA

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Legionella pneumophila (strain Paris)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501NucleophileUniRule annotation
    Sitei95 – 951Important for activityUniRule annotation
    Binding sitei105 – 1051SubstrateUniRule annotation
    Binding sitei116 – 1161SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi185 – 1906NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciLPNE297246:GCO9-2940-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTRUniRule annotation
    Gene namesi
    Name:hemAUniRule annotation
    Ordered Locus Names:lpp2283
    OrganismiLegionella pneumophila (strain Paris)
    Taxonomic identifieri297246 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

    Organism-specific databases

    LegioListilpp2283.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Glutamyl-tRNA reductasePRO_1000004630Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi297246.lpp2283.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5X2V4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni110 – 1123Substrate bindingUniRule annotation

    Domaini

    Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    Q5X2V4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVFVACGLNH KTAPIHVREK VALQPAMQDS LLSSLLDLPE VNEAAILSTC    50
    NRTEIYCDTN TPEVLGNWLA HEHQLSEELL SQFLYIHQGK EGIKHTLRVA 100
    SGLDSMMIGE PQILGQMKQA YQHACRLGTV KTQLRPVFEY IFRASKRIRT 150
    RSGIGANPVS IAYAAVQLIG QLFKNYHSLS VFLIGSGETA SLVAKYLHQH 200
    GVHRFLIASR TLENAQKLAE TFGGKTLSIG DIPQYLPLAD VVISATACPL 250
    PFINKSLVEH ALEQRNHAPM FLLDLAVPRD IEGNVNELEQ VHLYNVDDLQ 300
    SMIEKGMDER RNAALQAEQL IESELDNYIR WHRSLRAKDV ICDYRNQMHT 350
    LAQQELQRAL KKISAGQNQQ DVLNEFSMRL VNKLTHNPTI GLRQIAWDNR 400
    EDLLDLARYL FDTTANQSLY EEIS 424
    Length:424
    Mass (Da):47,884
    Last modified:November 23, 2004 - v1
    Checksum:iA5463608F99FC4E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628336 Genomic DNA. Translation: CAH13436.1.
    RefSeqiWP_015444133.1. NC_006368.1.
    YP_124594.1. NC_006368.1.

    Genome annotation databases

    EnsemblBacteriaiCAH13436; CAH13436; lpp2283.
    GeneIDi3119288.
    KEGGilpp:lpp2283.
    PATRICi22325133. VBILegPne27771_2605.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628336 Genomic DNA. Translation: CAH13436.1 .
    RefSeqi WP_015444133.1. NC_006368.1.
    YP_124594.1. NC_006368.1.

    3D structure databases

    ProteinModelPortali Q5X2V4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 297246.lpp2283.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH13436 ; CAH13436 ; lpp2283 .
    GeneIDi 3119288.
    KEGGi lpp:lpp2283.
    PATRICi 22325133. VBILegPne27771_2605.

    Organism-specific databases

    LegioListi lpp2283.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci LPNE297246:GCO9-2940-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMi SSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
      Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
      Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Paris.

    Entry informationi

    Entry nameiHEM1_LEGPA
    AccessioniPrimary (citable) accession number: Q5X2V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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