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Q1LIF4

- HEM1_RALME

UniProt

Q1LIF4 - HEM1_RALME

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (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 sitei53 – 531NucleophileUniRule annotation
    Sitei105 – 1051Important for activityUniRule annotation
    Binding sitei115 – 1151SubstrateUniRule annotation
    Binding sitei126 – 1261SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi195 – 2006NADPUniRule 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

    BioCyciCMET266264:GJ5G-3421-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:Rmet_3200
    OrganismiRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
    Taxonomic identifieri266264 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000002429: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Glutamyl-tRNA reductasePRO_0000335063Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi266264.Rmet_3200.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1LIF4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 554Substrate bindingUniRule annotation
    Regioni120 – 1223Substrate 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.
    HOGENOMiHOG000109650.
    KOiK02492.
    OrthoDBiEOG6MWNBM.

    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.

    Q1LIF4-1 [UniParc]FASTAAdd to Basket

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    MQLLAIGINH TTAPVSLRER VAFPLEQIKP ALGALRTHLS GRNGTEAAIL    50
    STCNRTEIYC ATDVLKPGEE GFEHTLRWLA QHHNVPASEL APHLYALPQS 100
    EAVRHAFRVA SGLDSMVLGE TQILGQLKDA VRTAGEAGAL GTYLNQLFQR 150
    TFAVAKEVRG QTEIGAHSVS MAAAAVRLAQ RIFESVSTQR VLFIGAGEMI 200
    ELCATHFAAQ TPRQIVVANR TVERGEKLAE QLSEQGLTTQ AIRLQDLGDR 250
    LHEFDIVVSC TASSLPIIGL GAVERAVKRR KHRPIMMVDL AVPRDVEPEV 300
    ARLDDVFLYT VDDLGAVVRE GNALRQAAVA QAEAIIDSRV LNFMHWLETR 350
    SVVPVIRELQ SQGEAIRQAE VERARRMLAR GDDPAAVLEA LSGALTRKFL 400
    HGPTHALNHT QGEDREALLR LVPGLFRHSS HSER 434
    Length:434
    Mass (Da):47,578
    Last modified:May 20, 2008 - v2
    Checksum:iBA0C9499A38CCE3D
    GO

    Sequence cautioni

    The sequence ABF10072.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000352 Genomic DNA. Translation: ABF10072.1. Different initiation.
    RefSeqiYP_585341.1. NC_007973.1.

    Genome annotation databases

    EnsemblBacteriaiABF10072; ABF10072; Rmet_3200.
    GeneIDi4040034.
    KEGGirme:Rmet_3200.
    PATRICi20291047. VBIRalMet4734_3593.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000352 Genomic DNA. Translation: ABF10072.1 . Different initiation.
    RefSeqi YP_585341.1. NC_007973.1.

    3D structure databases

    ProteinModelPortali Q1LIF4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266264.Rmet_3200.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABF10072 ; ABF10072 ; Rmet_3200 .
    GeneIDi 4040034.
    KEGGi rme:Rmet_3200.
    PATRICi 20291047. VBIRalMet4734_3593.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CMET266264:GJ5G-3421-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CH34 / ATCC 43123 / DSM 2839.

    Entry informationi

    Entry nameiHEM1_RALME
    AccessioniPrimary (citable) accession number: Q1LIF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 71 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