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A4YD89

- HEM1_METS5

UniProt

A4YD89 - HEM1_METS5

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (29 May 2007)
      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 sitei53 – 531NucleophileUniRule annotation
    Sitei98 – 981Important for activityUniRule annotation
    Binding sitei108 – 1081SubstrateUniRule annotation
    Binding sitei119 – 1191SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi188 – 1936NADPUniRule 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

    BioCyciMSED399549:GH1O-227-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:Msed_0214
    OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
    Taxonomic identifieri399549 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
    ProteomesiUP000000242: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Glutamyl-tRNA reductasePRO_1000075413Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi399549.Msed_0214.

    Structurei

    3D structure databases

    ProteinModelPortaliA4YD89.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 554Substrate bindingUniRule annotation
    Regioni113 – 1153Substrate 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.
    HOGENOMiHOG000107850.
    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.

    A4YD89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPVNDIIDS YSAIVYTHKT VGVDKLASHY LGWNEIKELS KYYDGEMAVL    50
    QTCNRIEIYL FSRNESSVNE ILHYLNEVHN KVISTDATIL RGEEAIKHLF 100
    EVASGIDSLS VGEYEILKQI KDAMRDSIKL GIGSRYIRAL LERSLKVGRR 150
    VRLETGISRG KVGVYSLAVE FAKSRFGDIL GKKIAILGAG EIGGKLALIL 200
    HNEGATDVTI FNRTFERGRN LAIKYGYSYF PLDFSRLHNY DIIFSAIFYP 250
    EKVKAPEGTV VIDLGSPPVF EGSNVYTLKD LEELSKATLE ERQREIERAE 300
    SIIREGLEEF RKDCLNLVYD NFVSSFMSRV EETRKEEVER ALKVLGDDGE 350
    ETREVLEAMT RSMIKKIFSP MFQNLRRAVE NNEINYINLA TSLLTHGGIS 400
    QDKTKEIKTE QEYKGRSSGD ETDS 424
    Length:424
    Mass (Da):48,090
    Last modified:May 29, 2007 - v1
    Checksum:i3E18D902434B5E92
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000682 Genomic DNA. Translation: ABP94391.1.
    RefSeqiWP_011921359.1. NC_009440.1.
    YP_001190315.1. NC_009440.1.

    Genome annotation databases

    EnsemblBacteriaiABP94391; ABP94391; Msed_0214.
    GeneIDi5104080.
    KEGGimse:Msed_0214.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000682 Genomic DNA. Translation: ABP94391.1 .
    RefSeqi WP_011921359.1. NC_009440.1.
    YP_001190315.1. NC_009440.1.

    3D structure databases

    ProteinModelPortali A4YD89.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 399549.Msed_0214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP94391 ; ABP94391 ; Msed_0214 .
    GeneIDi 5104080.
    KEGGi mse:Msed_0214.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000107850.
    KOi K02492.
    OMAi EHMIEDE.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MSED399549:GH1O-227-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 sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
      Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
      Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51363 / DSM 5348.

    Entry informationi

    Entry nameiHEM1_METS5
    AccessioniPrimary (citable) accession number: A4YD89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 61 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