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A4WJE1

- HEM11_PYRAR

UniProt

A4WJE1 - HEM11_PYRAR

Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (29 May 2007)
      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 sitei46 – 461NucleophileUniRule annotation
    Sitei86 – 861Important for activityUniRule annotation
    Binding sitei96 – 961SubstrateUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi175 – 1806NADPUniRule 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

    BioCyciPARS340102:GHGQ-939-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTR 1UniRule annotation
    Gene namesi
    Name:hemA1UniRule annotation
    Ordered Locus Names:Pars_0928
    OrganismiPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
    Taxonomic identifieri340102 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    ProteomesiUP000001567: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387Glutamyl-tRNA reductase 1PRO_0000335096Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi340102.Pars_0928.

    Structurei

    3D structure databases

    ProteinModelPortaliA4WJE1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate bindingUniRule annotation
    Regioni101 – 1033Substrate 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.
    OMAiVANGVHR.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    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]
    SUPFAMiSSF69742. SSF69742. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A4WJE1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLVNGLVAL SLTHKELGVD ELSKVANGVH RVCVSLRQPL FVLHTCNRVE    50
    AYLYNPPDEV VEIVKSGYAP YVEKVVERRG VDAARHLFRV AAGLESMLIG 100
    ETDVLGQLEE AFDRQVRAGY TRELLKTVVE RAIRVGKRVR TETGISRGPR 150
    GLGSLSILYV KEKIDLTNAR VCVIGAGSVG RGLVKELIDA GARRLVVVNR 200
    SVEKAADLGV EVWPLSERSV ERCLEDFDVV FTAVATFEPI IKSVPRDARV 250
    RIIVDMGMPR NTAAGLPVEV VTIDSLRDLA DRFNAMRDAE IKKAEEIVEE 300
    ELVALERLLR IRWVEEVSAK LLEYWFKIAE EEGERAGGLE AKIAARTTVK 350
    RTLLPVVNYL KKVAVSDIDE AYRIISVLRL SYGLKDL 387
    Length:387
    Mass (Da):43,082
    Last modified:May 29, 2007 - v1
    Checksum:iD8AFB667A047C5FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000660 Genomic DNA. Translation: ABP50508.1.
    RefSeqiWP_011900415.1. NC_009376.1.
    YP_001153160.1. NC_009376.1.

    Genome annotation databases

    EnsemblBacteriaiABP50508; ABP50508; Pars_0928.
    GeneIDi5054302.
    KEGGipas:Pars_0928.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000660 Genomic DNA. Translation: ABP50508.1 .
    RefSeqi WP_011900415.1. NC_009376.1.
    YP_001153160.1. NC_009376.1.

    3D structure databases

    ProteinModelPortali A4WJE1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 340102.Pars_0928.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP50508 ; ABP50508 ; Pars_0928 .
    GeneIDi 5054302.
    KEGGi pas:Pars_0928.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PARS340102:GHGQ-939-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    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 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 13514 / JCM 11321.

    Entry informationi

    Entry nameiHEM11_PYRAR
    AccessioniPrimary (citable) accession number: A4WJE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 59 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