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B1YBN0

- HEM1_PYRNV

UniProt

B1YBN0 - HEM1_PYRNV

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (20 May 2008)
      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 sitei48 – 481NucleophileUniRule annotation
    Sitei88 – 881Important for activityUniRule annotation
    Binding sitei98 – 981SubstrateUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi177 – 1826NADPUniRule 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

    BioCyciTNEU444157:GHL2-1966-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:Tneu_1917
    OrganismiPyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus)
    Taxonomic identifieri444157 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    ProteomesiUP000001694: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Glutamyl-tRNA reductasePRO_1000093175Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi444157.Tneu_1917.

    Structurei

    3D structure databases

    ProteinModelPortaliB1YBN0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 504Substrate bindingUniRule annotation
    Regioni103 – 1053Substrate 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.
    HOGENOMiHOG000112880.
    KOiK02492.
    OMAiYREADAN.

    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.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B1YBN0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLLAPLSAV VLTYREVSAE ALGKVGQEMK RCIERRARAF PMYVLHTCSR    50
    VEAYLYGAPP EEVQEVAEAY RRYVDSVRVI TGAEAARHLF RVAAGLDSIL 100
    IGETDVLGQV EEAFDRQVRA GYTRGLLKTV VERAVRVGKR VRTETAISRG 150
    PRGLGSLSII YVSRLLDLRQ AKAAVLGAGA VGSGLAMELA SRGVGKLYIL 200
    NRTFEKAREV AAKTGGEARP LTREEVERCL RECDVVFSSV HSMEYVIDRV 250
    PEGASVKIVV DLGVPQTVAP GLPVKVVRIE DLRQVAEQYN AERAAEVAKA 300
    EAIVEEELAA LPRLLARRYV EETVAALLET AMTAAEEEGA RAGCDAAALA 350
    AKTTVKRVLL PLVEKMKKMA EDGQMEEAVR LANVLTQAVG RKT 393
    Length:393
    Mass (Da):42,756
    Last modified:May 20, 2008 - v1
    Checksum:i27D03C3CC36DF232
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001014 Genomic DNA. Translation: ACB40832.1.
    RefSeqiWP_012351251.1. NC_010525.1.
    YP_001795278.1. NC_010525.1.

    Genome annotation databases

    EnsemblBacteriaiACB40832; ACB40832; Tneu_1917.
    GeneIDi6164814.
    KEGGitne:Tneu_1917.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001014 Genomic DNA. Translation: ACB40832.1 .
    RefSeqi WP_012351251.1. NC_010525.1.
    YP_001795278.1. NC_010525.1.

    3D structure databases

    ProteinModelPortali B1YBN0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 444157.Tneu_1917.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB40832 ; ACB40832 ; Tneu_1917 .
    GeneIDi 6164814.
    KEGGi tne:Tneu_1917.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000112880.
    KOi K02492.
    OMAi YREADAN.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci TNEU444157:GHL2-1966-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.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2338 / JCM 9278 / V24Sta.

    Entry informationi

    Entry nameiHEM1_PYRNV
    AccessioniPrimary (citable) accession number: B1YBN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 51 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