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A1RQP7

- HEM1_PYRIL

UniProt

A1RQP7 - HEM1_PYRIL

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189)
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 (06 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 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

    BioCyciPISL384616:GC8H-98-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:Pisl_0096
    OrganismiPyrobaculum islandicum (strain DSM 4184 / JCM 9189)
    Taxonomic identifieri384616 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    ProteomesiUP000002595: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Glutamyl-tRNA reductasePRO_1000004679Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi384616.Pisl_0096.

    Structurei

    3D structure databases

    ProteinModelPortaliA1RQP7.
    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.

    A1RQP7-1 [UniParc]FASTAAdd to Basket

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    MDLLSPLSAI VLTYREVDTD TLGKIGEEMR KCLEQMGRGT PIYVLHTCGR    50
    VEAYLYGASP EEVQTVAETY RKYVNSVRII AGVEAARHLF RVAAGLDSML 100
    IGETDVLGQL EEAFDRQVRA GYTRGLLKTI VERAVRVGKR VRTETAISRG 150
    PRGLGSLSII YVSRLLDMRQ AKVAVLGAGA VGAGLAMELA ARGVKKLYIL 200
    NRTLEKAKEV AAKTGGEARP LTKEEVERCL RECDVVFSSV HSMEYIIDKI 250
    PEGASVKVVV DLGVPQTVAS GLPVKVVRIE DLREIAEQYN AERASEIAKA 300
    EAIVEEELAI LPKLLARRYI EETVSTFIET AMLAAEEEGA RAGCNTATLA 350
    ARTTVKRILL PLVERLKKMA EDGQIEEAVK LAQMLSQTIG RKI 393
    Length:393
    Mass (Da):43,011
    Last modified:February 6, 2007 - v1
    Checksum:iD5B0DC67046AF16A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000504 Genomic DNA. Translation: ABL87279.1.
    RefSeqiWP_011761856.1. NC_008701.1.
    YP_929622.1. NC_008701.1.

    Genome annotation databases

    EnsemblBacteriaiABL87279; ABL87279; Pisl_0096.
    GeneIDi4616972.
    KEGGipis:Pisl_0096.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000504 Genomic DNA. Translation: ABL87279.1 .
    RefSeqi WP_011761856.1. NC_008701.1.
    YP_929622.1. NC_008701.1.

    3D structure databases

    ProteinModelPortali A1RQP7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 384616.Pisl_0096.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL87279 ; ABL87279 ; Pisl_0096 .
    GeneIDi 4616972.
    KEGGi pis:Pisl_0096.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PISL384616:GC8H-98-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. "Complete sequence of Pyrobaculum islandicum DSM 4184."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
      , Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 4184 / JCM 9189.

    Entry informationi

    Entry nameiHEM1_PYRIL
    AccessioniPrimary (citable) accession number: A1RQP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: February 6, 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