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B0R6C0

- HEM1_HALS3

UniProt

B0R6C0 - HEM1_HALS3

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (08 Apr 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 sitei53 – 531NucleophileUniRule annotation
    Sitei95 – 951Important for activityUniRule annotation
    Binding sitei105 – 1051SubstrateUniRule annotation
    Binding sitei116 – 1161SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi184 – 1896NADPUniRule 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

    BioCyciHSAL478009:GJVF-1440-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:OE_3496R
    OrganismiHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
    Taxonomic identifieri478009 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium
    ProteomesiUP000001321: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Glutamyl-tRNA reductasePRO_1000093142Add
    BLAST

    Proteomic databases

    PRIDEiB0R6C0.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi478009.OE3496R.

    Structurei

    3D structure databases

    ProteinModelPortaliB0R6C0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 554Substrate 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.
    HOGENOMiHOG000109651.
    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]
    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.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B0R6C0-1 [UniParc]FASTAAdd to Basket

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    MNGNTGVVSG VRVSHETASL DELAAASAAS TEAALDALLE QPPVEEAFVL    50
    QTCHRVEAYV VTADQASGRR ALGGAGFNPA GGGAISMGHE DSLRHLLRVA 100
    AGLESLVVGE DQILGQLRDA YDAAKDAGGI DHVLREAVTK AMHVGERART 150
    ETAINEGATS LGTAAVRLAE RKTQLADARA VVVGAGEMGA LAAKAFASAT 200
    VAEIVIANRT PARAVRVADM VSVPAEATTL ADARGRLDAA DVVVTATGSP 250
    EHVLPASAFA DAGDTVVVDL AQPRDVAPGA GGHDGVAVHD LDDLEAVTAA 300
    TRERREDAAR EVEAMIETEF ERLLTQYKRK RADEVIARMY ESADRLKSRE 350
    VQTAVHRLEA ESGSLSADER EVVESMADAL VSQLLAAPTK SLRDAAAEDD 400
    WSTIATALEL FNPEFEDGMP FDASRGGDAA SAESED 436
    Length:436
    Mass (Da):45,450
    Last modified:April 8, 2008 - v1
    Checksum:i3016F114705F6987
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM774415 Genomic DNA. Translation: CAP14289.1.
    RefSeqiYP_001689635.1. NC_010364.1.

    Genome annotation databases

    EnsemblBacteriaiCAP14289; CAP14289; OE_3496R.
    GeneIDi5953600.
    KEGGihsl:OE3496R.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM774415 Genomic DNA. Translation: CAP14289.1 .
    RefSeqi YP_001689635.1. NC_010364.1.

    3D structure databases

    ProteinModelPortali B0R6C0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 478009.OE3496R.

    Proteomic databases

    PRIDEi B0R6C0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAP14289 ; CAP14289 ; OE_3496R .
    GeneIDi 5953600.
    KEGGi hsl:OE3496R.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi YREADAN.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci HSAL478009:GJVF-1440-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 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.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
      Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
      Genomics 91:335-346(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29341 / DSM 671 / R1.

    Entry informationi

    Entry nameiHEM1_HALS3
    AccessioniPrimary (citable) accession number: B0R6C0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 54 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