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A5ULU4

- HEM1_METS3

UniProt

A5ULU4 - HEM1_METS3

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (10 Jul 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 sitei46 – 461NucleophileUniRule annotation
    Sitei83 – 831Important for activityUniRule annotation
    Binding sitei93 – 931SubstrateUniRule annotation
    Binding sitei104 – 1041SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi173 – 1786NADPUniRule 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

    BioCyciMSMI420247:GHWZ-992-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:Msm_0967
    OrganismiMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861)
    Taxonomic identifieri420247 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobrevibacter
    ProteomesiUP000001992: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 399399Glutamyl-tRNA reductasePRO_1000004642Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi420247.Msm_0967.

    Structurei

    3D structure databases

    ProteinModelPortaliA5ULU4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate 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.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiKMLHGTM.

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A5ULU4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MILNLRVDHK IANIDAMENI AKEMDQLFLE LQEKYSIVEY VEISTCNRKE    50
    YYIHNDNIDA SDSLLSHENK SIIIDYGDSV IKHLFRMTSG LESMIVGEDQ 100
    ILGQVSDAKQ KAFKERHCGK ILDSIFTKAI HVGRVVRNKT NINKGSISIG 150
    SAAVDLAEKH LGNLENKSVL VIGAGKMGKL VAKALAEKNL NAIFVANRTY 200
    YVAVELANDL NGHAVLFNEL GKYVQTADLI ISATGAPHYI LNKERLEKTD 250
    GDFKDLLMID IANPRDICED VCELGVKLFN IDDLREIADE NTKLRKKEFA 300
    EAENIIDEEF SLLKESFKLI GVEDIIANLR VSMENIRERE TEKAIAKLSD 350
    VDANAKIIDN LTNSIVNKIF FDISKKIKQA AHENDEELIR AIEFMFEEK 399
    Length:399
    Mass (Da):44,990
    Last modified:July 10, 2007 - v1
    Checksum:iF2BB1E52489E6504
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000678 Genomic DNA. Translation: ABQ87172.1.
    RefSeqiWP_011954208.1. NC_009515.1.
    YP_001273540.1. NC_009515.1.

    Genome annotation databases

    EnsemblBacteriaiABQ87172; ABQ87172; Msm_0967.
    GeneIDi5217012.
    KEGGimsi:Msm_0967.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000678 Genomic DNA. Translation: ABQ87172.1 .
    RefSeqi WP_011954208.1. NC_009515.1.
    YP_001273540.1. NC_009515.1.

    3D structure databases

    ProteinModelPortali A5ULU4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 420247.Msm_0967.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ87172 ; ABQ87172 ; Msm_0967 .
    GeneIDi 5217012.
    KEGGi msi:Msm_0967.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MSMI420247:GHWZ-992-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PS / ATCC 35061 / DSM 861.

    Entry informationi

    Entry nameiHEM1_METS3
    AccessioniPrimary (citable) accession number: A5ULU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 56 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