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Q3ING1

- HEM1_NATPD

UniProt

Q3ING1 - HEM1_NATPD

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium pharaonis)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      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
    Sitei95 – 951Important for activityUniRule annotation
    Binding sitei105 – 1051SubstrateUniRule annotation
    Binding sitei116 – 1161SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi184 – 1896NADPUniRule 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

    BioCyciNPHA348780:GJX0-2285-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:NP_4502A
    OrganismiNatronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium pharaonis)
    Taxonomic identifieri348780 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas
    ProteomesiUP000002698: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Glutamyl-tRNA reductasePRO_1000004654Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi348780.NP4502A.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3ING1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 554Substrate bindingUniRule annotation
    Regioni110 – 1123Substrate 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.
    OMAiHEVTGEY.

    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.

    Q3ING1-1 [UniParc]FASTAAdd to Basket

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    MTVETGIVVG ASVSHSHASI DQIETAADGS QQTAVEELLS KEGVSEAFVL    50
    QTCNRAEAYV VANDSETGTA ALAGYLAGVD DDAIRMLSHN QSLKHLMAVA 100
    CGLESLVIGE DQILGQVRDA YEDARGVGGV GPTLNDAVLK ALHVGERART 150
    ETAINEGAVS LGSAAVRFAA ERHGVTGSTA LVVGAGEMAT LAAKALDDPA 200
    SRVIVANRTR ERAERLAEEL STTASVVGVD SVDEAADAAD VVVSATGSED 250
    YVIDTADLGG VGETCVLDIA QPRDVAPGAD GIDGVAVYDL DTIESVTDEA 300
    RAKRREAAET VETMIDEEFE HLMTQYKRKR ADQVIAAMYE GAERIKAREL 350
    RTAVSKFEAE REDGLSEREH EIVESMADAL VGQLLSAPTQ SLRDAAEEDD 400
    WATINAALQL FGPGLEPEPT ELPTVPDGPE GVPEELRERM SSGMLEQFST 450
    NDD 453
    Length:453
    Mass (Da):47,809
    Last modified:November 8, 2005 - v1
    Checksum:i839ADF48145910A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR936257 Genomic DNA. Translation: CAI50342.1.
    RefSeqiWP_011323957.1. NC_007426.1.
    YP_330979.1. NC_007426.1.

    Genome annotation databases

    EnsemblBacteriaiCAI50342; CAI50342; NP_4502A.
    GeneIDi3702804.
    KEGGinph:NP4502A.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR936257 Genomic DNA. Translation: CAI50342.1 .
    RefSeqi WP_011323957.1. NC_007426.1.
    YP_330979.1. NC_007426.1.

    3D structure databases

    ProteinModelPortali Q3ING1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 348780.NP4502A.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAI50342 ; CAI50342 ; NP_4502A .
    GeneIDi 3702804.
    KEGGi nph:NP4502A.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi HEVTGEY.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci NPHA348780:GJX0-2285-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. "Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
      Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
      Genome Res. 15:1336-1343(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35678 / DSM 2160.

    Entry informationi

    Entry nameiHEM1_NATPD
    AccessioniPrimary (citable) accession number: Q3ING1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 77 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