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A2BJB7

- HEM1_HYPBU

UniProt

A2BJB7 - HEM1_HYPBU

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (20 Feb 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 sitei50 – 501NucleophileUniRule annotation
    Sitei89 – 891Important for activityUniRule annotation
    Binding sitei99 – 991SubstrateUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi179 – 1846NADPUniRule 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

    BioCyciHBUT415426:GC56-206-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:Hbut_0206
    OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)
    Taxonomic identifieri415426 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
    ProteomesiUP000002593: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 411411Glutamyl-tRNA reductasePRO_0000335089Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi415426.Hbut_0206.

    Structurei

    3D structure databases

    ProteinModelPortaliA2BJB7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni104 – 1063Substrate 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.
    KOiK02492.
    OMAiEHMIEDE.

    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.

    Sequencei

    Sequence statusi: Complete.

    A2BJB7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRLLEELTA VILTHRDAPL DVVGSFESRV GEAYQILRGV VDEAVVLATC    50
    NRFEVYALPR RGFVETVIGF LGEASRYARI LHGMDVVRHL FRVAAGLESA 100
    IIGENEILGQ VARAYEEARR RGVAGKYLGL LFSQAVRTGK LVRSRTRISY 150
    GNVGAPGAAV KLAREAAGGF DGKHVVVVGA GEAGSIMASL VREEAPTARI 200
    SIVNRSVDRA RELAGKVRGE AYGLDMLPKL LAAADVVLVA VTVNEPVIKR 250
    SMLEDVGRHL VVVDISNPPA VEQPIPSNVY YAGLRDVEKV IKEVLAVRIR 300
    EVPKAEAIVE EQVALLRKLW LKRGADEAIA EIMRYANRVM EEEVEELVSR 350
    LRGLGVDGAA LLVARSFAYS LTKKLLRPLI LYAHEAALEG SLSKLEEIAQ 400
    KYRDELARRQ H 411
    Length:411
    Mass (Da):45,007
    Last modified:February 20, 2007 - v1
    Checksum:iC744C393B3D4C4FE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000493 Genomic DNA. Translation: ABM80078.1.
    RefSeqiWP_011821395.1. NC_008818.1.
    YP_001012423.1. NC_008818.1.

    Genome annotation databases

    EnsemblBacteriaiABM80078; ABM80078; Hbut_0206.
    GeneIDi4782332.
    KEGGihbu:Hbut_0206.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000493 Genomic DNA. Translation: ABM80078.1 .
    RefSeqi WP_011821395.1. NC_008818.1.
    YP_001012423.1. NC_008818.1.

    3D structure databases

    ProteinModelPortali A2BJB7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 415426.Hbut_0206.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM80078 ; ABM80078 ; Hbut_0206 .
    GeneIDi 4782332.
    KEGGi hbu:Hbut_0206.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi EHMIEDE.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci HBUT415426:GC56-206-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. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
      Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
      Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 5456 / JCM 9403.

    Entry informationi

    Entry nameiHEM1_HYPBU
    AccessioniPrimary (citable) accession number: A2BJB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 65 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, Reference proteome

    Documents

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

    External Data

    Dasty 3