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B2A1G4

- HEM1_NATTJ

UniProt

B2A1G4 - HEM1_NATTJ

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (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 sitei50 – 501NucleophileUniRule annotation
    Sitei101 – 1011Important for activityUniRule annotation
    Binding sitei111 – 1111SubstrateUniRule annotation
    Binding sitei122 – 1221SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi191 – 1966NADPUniRule 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

    BioCyciNTHE457570:GHRL-1148-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:Nther_1121
    OrganismiNatranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
    Taxonomic identifieri457570 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaNatranaerobialesNatranaerobiaceaeNatranaerobius
    ProteomesiUP000001683: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Glutamyl-tRNA reductasePRO_1000093153Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi457570.Nther_1121.

    Structurei

    3D structure databases

    ProteinModelPortaliB2A1G4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni116 – 1183Substrate 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.
    OMAiLAHKLTN.
    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.
    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.

    B2A1G4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MILAVIGINH ETASVETREQ LAFSSKQVKE LVQKLIEGQP IKEASVLSTC    50
    NRTEVHFTVN TGQIEAGKNH IMTYLSDFSD LDPREYVDHL YFITDQEAVS 100
    HIFKVTAGLN SLVTGETEIL GQVKKAYQLS DEAGGVDSIF HGLYQQALRT 150
    GKRVHRETGI NDNAASVSYA SVELATKIFG SLQNRRALII GAGKMSELAA 200
    RHLYSNGVKD VIVINRTIER AKNLADKFGG LYASYDQLSE WLNEIDIVIT 250
    STGAPHFVIK EEQIKRAMKS RKYSPMFLID IAVPRDVEPS VNNQDNAYLY 300
    TIDDLEAVVE SNMQERQEEA RNAELIISEE VAEFMVWYKT RDVVPLISAL 350
    REKAEDVRKM ELEKYHKKLK NLSPKEQEAV DKLTKSIVNK ILKEPVLRIK 400
    EFAVEDKSEL YMATLAQLFD LEDEVIPKDG EEHSSSKEVE SVTQSSTERG 450
    HHESDFHN 458
    Length:458
    Mass (Da):51,692
    Last modified:May 20, 2008 - v1
    Checksum:iAE53385E112E0088
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001034 Genomic DNA. Translation: ACB84704.1.
    RefSeqiYP_001917292.1. NC_010718.1.

    Genome annotation databases

    EnsemblBacteriaiACB84704; ACB84704; Nther_1121.
    GeneIDi6315350.
    KEGGinth:Nther_1121.
    PATRICi22670894. VBINatThe92436_1156.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001034 Genomic DNA. Translation: ACB84704.1 .
    RefSeqi YP_001917292.1. NC_010718.1.

    3D structure databases

    ProteinModelPortali B2A1G4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 457570.Nther_1121.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB84704 ; ACB84704 ; Nther_1121 .
    GeneIDi 6315350.
    KEGGi nth:Nther_1121.
    PATRICi 22670894. VBINatThe92436_1156.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci NTHE457570:GHRL-1148-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. "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-LF."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
      , Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.
      Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF.

    Entry informationi

    Entry nameiHEM1_NATTJ
    AccessioniPrimary (citable) accession number: B2A1G4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 51 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