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Q18F28

- HEM1_HALWD

UniProt

Q18F28 - HEM1_HALWD

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (25 Jul 2006)
      Previous versions | rss
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    • Comment

    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 sitei51 – 511NucleophileUniRule annotation
    Sitei93 – 931Important for activityUniRule annotation
    Binding sitei103 – 1031SubstrateUniRule annotation
    Binding sitei114 – 1141SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi182 – 1876NADPUniRule 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

    BioCyciHWAL362976:GJSR-2460-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:HQ_3336A
    OrganismiHaloquadratum walsbyi (strain DSM 16790 / HBSQ001)
    Taxonomic identifieri362976 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum
    ProteomesiUP000001975: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Glutamyl-tRNA reductasePRO_0000335088Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi362976.HQ3336A.

    Structurei

    3D structure databases

    ProteinModelPortaliQ18F28.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate bindingUniRule annotation
    Regioni108 – 1103Substrate 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.
    OMAiEHMIEDE.

    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.

    Q18F28-1 [UniParc]FASTAAdd to Basket

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    MNTGVICGVR VSHNRASVEE IELAGERDSR TIMETLLTRD GITESFAIQT    50
    CNRSEAYVVA DGAVAGRRAL ASFAPDVRDG AVVDMSHEES LRHLLRVATG 100
    LESLVLGEDQ ILGQFKRAIE VARGIGALGP MLEAGVTKAI HVGERARSET 150
    SINEGAVSIG SAAVRLAGQS VGLNGRKALV IGAGEMGSLV AESLASTNIS 200
    EVVIANRTIE NAESIAETIN SPAYAVSLDS LTEVITEASI IMTATGYGKY 250
    LIEPTDIDGA GETFIIDLAQ PRNVHPATAD IENAIVQDID ALESITKETE 300
    ASRQAAAREV DAMIDEEFDR LLESYKRQRA DEAISEMYEA AEHVKRREVE 350
    TALEKLEKQG TLTDNQRETI SSMADTLINQ LLAAPTKSLR DAAAEDDWTT 400
    IQTAMTLFDP NFGGDTPQPD RPDDIPRAAE RGDISGDDLP DDVPNHIAEK 450
    VSDG 454
    Length:454
    Mass (Da):48,625
    Last modified:July 25, 2006 - v1
    Checksum:i2D20D329DCA6FDDC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM180088 Genomic DNA. Translation: CAJ53433.1.
    RefSeqiWP_011572535.1. NC_008212.1.
    YP_659025.1. NC_008212.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ53433; CAJ53433; HQ_3336A.
    GeneIDi4194102.
    KEGGihwa:HQ3336A.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM180088 Genomic DNA. Translation: CAJ53433.1 .
    RefSeqi WP_011572535.1. NC_008212.1.
    YP_659025.1. NC_008212.1.

    3D structure databases

    ProteinModelPortali Q18F28.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 362976.HQ3336A.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ53433 ; CAJ53433 ; HQ_3336A .
    GeneIDi 4194102.
    KEGGi hwa:HQ3336A.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci HWAL362976:GJSR-2460-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. "The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
      Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
      BMC Genomics 7:169-169(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 16790 / HBSQ001.

    Entry informationi

    Entry nameiHEM1_HALWD
    AccessioniPrimary (citable) accession number: Q18F28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 75 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