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Q1IWG2

- HEM1_DEIGD

UniProt

Q1IWG2 - HEM1_DEIGD

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Deinococcus geothermalis (strain DSM 11300)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (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 sitei54 – 541NucleophileUniRule annotation
    Sitei95 – 951Important for activityUniRule annotation
    Binding sitei105 – 1051SubstrateUniRule annotation
    Binding sitei116 – 1161SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi185 – 1906NADPUniRule 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

    BioCyciDGEO319795:GHMU-2176-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:Dgeo_2128
    OrganismiDeinococcus geothermalis (strain DSM 11300)
    Taxonomic identifieri319795 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
    ProteomesiUP000002431: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 349349Glutamyl-tRNA reductasePRO_0000335027Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi319795.Dgeo_2128.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1IWG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 564Substrate 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.
    OrthoDBiEOG6MWNBM.

    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]
    PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMiSSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q1IWG2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPLAPLDFA VIGLNHQTAP VEVREQAAVR AGDEGKVLQH LSRYAREVML    50
    LNTCNRTEVY LAGLQGDPLR AFESGWGRAL DGHLYVHRGE AAATHLYRVA 100
    AGLDSLVIGE TQIQGQVKRA WQEAHARGLS GTLLNKVAQG ALAAGKRVRS 150
    ETGLSDKVVS VSSAAVELAE AALGELRHRT ALILGAGETA ELTLTHLRAA 200
    GVQDVIVVNR TEARARQLAD KLGGRACAAE YLHEVLPEAD VVIASSAAPH 250
    YVLHGEGVRA ALAKRPERPI FLIDISVPRI LDPDIRAVSG AHLYNLDDLT 300
    AIVSRNLQSR RAALPYAEAI IREAVADLLR WHLTREAQLG RRAVALASD 349
    Length:349
    Mass (Da):37,531
    Last modified:May 20, 2008 - v2
    Checksum:i9B1FA1D2703A99E9
    GO

    Sequence cautioni

    The sequence ABF46422.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000359 Genomic DNA. Translation: ABF46422.1. Different initiation.
    RefSeqiYP_605591.1. NC_008025.1.

    Genome annotation databases

    EnsemblBacteriaiABF46422; ABF46422; Dgeo_2128.
    GeneIDi4058863.
    KEGGidge:Dgeo_2128.
    PATRICi21626231. VBIDeiGeo41128_2727.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000359 Genomic DNA. Translation: ABF46422.1 . Different initiation.
    RefSeqi YP_605591.1. NC_008025.1.

    3D structure databases

    ProteinModelPortali Q1IWG2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 319795.Dgeo_2128.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABF46422 ; ABF46422 ; Dgeo_2128 .
    GeneIDi 4058863.
    KEGGi dge:Dgeo_2128.
    PATRICi 21626231. VBIDeiGeo41128_2727.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci DGEO319795:GHMU-2176-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 ]
    PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMi SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 11300.

    Entry informationi

    Entry nameiHEM1_DEIGD
    AccessioniPrimary (citable) accession number: Q1IWG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 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