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Q6L0J9

- HEM1_PICTO

UniProt

Q6L0J9 - HEM1_PICTO

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
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 sitei50 – 501NucleophileUniRule annotation
    Sitei82 – 821Important for activityUniRule annotation
    Binding sitei92 – 921SubstrateUniRule annotation
    Binding sitei103 – 1031SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi171 – 1766NADPUniRule 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

    BioCyciPTOR263820:GHA3-959-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:PTO0918
    OrganismiPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
    Taxonomic identifieri263820 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus
    ProteomesiUP000000438: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 401401Glutamyl-tRNA reductasePRO_0000114107Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi263820.PTO0918.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6L0J9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni97 – 993Substrate 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.
    HOGENOMiHOG000112884.
    KOiK02492.
    OMAiYREADAN.

    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.

    Q6L0J9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIIMIPIYAI TWNFRDTPEG FDKIVNNDYN YFESLCKKSS IDEFVILITC    50
    NRVEIYAYTR NEIDKDLFKD SLIYNYPEST MHLLRVASGL ESMSIGENDI 100
    MRQVKEAYEL SIKRKTSGKI LSYIFKKALN VGKEVRTQTS ISRGKTSIPA 150
    ISLDICDNEY GINNKSILII GNGKMATDFS RYLKEYRPGN VTIAGRSIDH 200
    ARNLAVLYGY SYDSIKNLNN LIKNSDIIIA ATSAGNYIVK DLGDLARNKY 250
    FIDISKPENI DPEISKYARL LSINEIGKIL KRNEDEKKGE VEIAEVIINQ 300
    EQKTIDEKLK EMMLDDVIAM FYKFANNVKK DELEELFLIQ DFNDEQKKDI 350
    DAMTSSLINK ILAPYTNSVK QFIKENKNFD YILNEYKKML EQFMENIVKK 400
    L 401
    Length:401
    Mass (Da):46,302
    Last modified:July 5, 2004 - v1
    Checksum:iC16EDBDE1B47E975
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017261 Genomic DNA. Translation: AAT43503.1.
    RefSeqiYP_023696.1. NC_005877.1.

    Genome annotation databases

    EnsemblBacteriaiAAT43503; AAT43503; PTO0918.
    GeneIDi2843948.
    KEGGipto:PTO0918.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017261 Genomic DNA. Translation: AAT43503.1 .
    RefSeqi YP_023696.1. NC_005877.1.

    3D structure databases

    ProteinModelPortali Q6L0J9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 263820.PTO0918.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT43503 ; AAT43503 ; PTO0918 .
    GeneIDi 2843948.
    KEGGi pto:PTO0918.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000112884.
    KOi K02492.
    OMAi YREADAN.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PTOR263820:GHA3-959-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: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

    Entry informationi

    Entry nameiHEM1_PICTO
    AccessioniPrimary (citable) accession number: Q6L0J9
    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, 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