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A3MW83

- HEM11_PYRCJ

UniProt

A3MW83 - HEM11_PYRCJ

Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (03 Apr 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 sitei43 – 431NucleophileUniRule annotation
    Sitei83 – 831Important for activityUniRule annotation
    Binding sitei93 – 931SubstrateUniRule annotation
    Binding sitei104 – 1041SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi172 – 1776NADPUniRule 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

    BioCyciPCAL410359:GIX2-1515-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTR 1UniRule annotation
    Gene namesi
    Name:hemA1UniRule annotation
    Ordered Locus Names:Pcal_1481
    OrganismiPyrobaculum calidifontis (strain JCM 11548 / VA1)
    Taxonomic identifieri410359 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    ProteomesiUP000001431: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380Glutamyl-tRNA reductase 1PRO_0000335098Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi410359.Pcal_1481.

    Structurei

    3D structure databases

    ProteinModelPortaliA3MW83.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 454Substrate bindingUniRule annotation
    Regioni98 – 1003Substrate 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.
    OMAiVANGVHR.

    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]
    SUPFAMiSSF69742. SSF69742. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A3MW83-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVDKLYALS LSHKRLSVDE LSEISRNVHK TCYNVQAFVF HTCNRVEVYL    50
    YDADAGPAEH IKRSYGPYVE KVAEFRGVEA ARHLFRVAAG LESMLIGETD 100
    VLGQLEEAYE SQVRRGNLRG LLKTVVERAV AVGKRVRTET GISRGPRGLG 150
    SLSIVYLSRR LPLREISVCV IGAGAVGRGV VKELIDAGVR RVAVVNRTVE 200
    KAADLGVEVR PLTSENVEWC LREFDVVYTA VSSFEPVVVY VPPGSRVKLV 250
    VDLGVPRNTA PNLPVEVVTL DHLRELAEEF NRQRAEEVSK AEKIVEEEVA 300
    RLEEVLRRRW VELEMSALLK KWFAVAEEEG ERAGGGPARL AAMSTVKRTL 350
    LPLVNYIKEV AVKDLAVAEG LLQVLKSAYA 380
    Length:380
    Mass (Da):42,139
    Last modified:April 3, 2007 - v1
    Checksum:i02E622F27C210096
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000561 Genomic DNA. Translation: ABO08900.1.
    RefSeqiYP_001056366.1. NC_009073.1.

    Genome annotation databases

    EnsemblBacteriaiABO08900; ABO08900; Pcal_1481.
    GeneIDi4910204.
    KEGGipcl:Pcal_1481.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000561 Genomic DNA. Translation: ABO08900.1 .
    RefSeqi YP_001056366.1. NC_009073.1.

    3D structure databases

    ProteinModelPortali A3MW83.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 410359.Pcal_1481.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO08900 ; ABO08900 ; Pcal_1481 .
    GeneIDi 4910204.
    KEGGi pcl:Pcal_1481.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PCAL410359:GIX2-1515-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 ]
    SUPFAMi SSF69742. SSF69742. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCM 11548 / VA1.

    Entry informationi

    Entry nameiHEM11_PYRCJ
    AccessioniPrimary (citable) accession number: A3MW83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 60 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