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Q72IJ0

- HEM1_THET2

UniProt

Q72IJ0 - HEM1_THET2

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 sitei47 – 471NucleophileUniRule annotation
    Sitei86 – 861Important for activityUniRule annotation
    Binding sitei96 – 961SubstrateUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi176 – 1816NADPUniRule 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

    BioCyciTTHE262724:GCAT-1155-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:TT_C1142
    OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
    Taxonomic identifieri262724 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000592: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 390390Glutamyl-tRNA reductasePRO_0000114080Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi262724.TTC1142.

    Structurei

    3D structure databases

    ProteinModelPortaliQ72IJ0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 494Substrate bindingUniRule annotation
    Regioni101 – 1033Substrate 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.
    KOiK02492.
    OMAiVANGVHR.
    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.

    Q72IJ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALPLYLVGL SHKTAPLEVR ERAALDPVVA LPAALSALGK GVVLSTCNRT    50
    ELYGVGSPEK ARAFLLSRGV VPRHLYVKEG VEALRHLYRV AAGLDSLVVG 100
    EAQILGQVRE ALFLARRQGA TESLLEKAFQ SAIALGKRAR SETGIGMGAV 150
    SVAYAALDLA LAVYGDLSGL SVAVLGAGEM AELFLTHLKA HGVGRILVVN 200
    RTEEKAQALA ERFGGEAFGL PALPQVLRQA DLVVASAAAP HYLVGPEDLP 250
    KRAKPLFLID IALPRNIDPR VGDLPHAYLY NLDDLKRVVD RNLRARAGEI 300
    PKVEALIEKA LGDYMEWYAG HRVREAIRAL EAWARVQAAK AQPEAGPVEL 350
    EKAAGRLAHP FILGLKRRAL DRVGGPPCPE DCLLYRLSRT 390
    Length:390
    Mass (Da):41,965
    Last modified:July 5, 2004 - v1
    Checksum:iBC12B897710ED086
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017221 Genomic DNA. Translation: AAS81484.1.
    RefSeqiWP_011173555.1. NC_005835.1.
    YP_005111.1. NC_005835.1.

    Genome annotation databases

    EnsemblBacteriaiAAS81484; AAS81484; TT_C1142.
    GeneIDi2775317.
    KEGGitth:TTC1142.
    PATRICi23952691. VBITheThe54392_1135.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017221 Genomic DNA. Translation: AAS81484.1 .
    RefSeqi WP_011173555.1. NC_005835.1.
    YP_005111.1. NC_005835.1.

    3D structure databases

    ProteinModelPortali Q72IJ0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262724.TTC1142.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS81484 ; AAS81484 ; TT_C1142 .
    GeneIDi 2775317.
    KEGGi tth:TTC1142.
    PATRICi 23952691. VBITheThe54392_1135.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi VANGVHR.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci TTHE262724:GCAT-1155-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: HB27 / ATCC BAA-163 / DSM 7039.

    Entry informationi

    Entry nameiHEM1_THET2
    AccessioniPrimary (citable) accession number: Q72IJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 79 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