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Q2S2A5

- HEM1_SALRD

UniProt

Q2S2A5 - HEM1_SALRD

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Salinibacter ruber (strain DSM 13855 / M31)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      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 sitei49 – 491NucleophileUniRule annotation
    Sitei94 – 941Important for activityUniRule annotation
    Binding sitei104 – 1041SubstrateUniRule annotation
    Binding sitei115 – 1151SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1946NADPUniRule 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

    BioCyciSRUB309807:GJJD-1552-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:SRU_1555
    OrganismiSalinibacter ruber (strain DSM 13855 / M31)
    Taxonomic identifieri309807 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter
    ProteomesiUP000008674: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 479479Glutamyl-tRNA reductasePRO_0000335070Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi309807.SRU_1555.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2S2A5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 514Substrate bindingUniRule annotation
    Regioni109 – 1113Substrate 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.
    HOGENOMiHOG000106238.
    KOiK02492.
    OrthoDBiEOG6MWNBM.

    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.

    Q2S2A5-1 [UniParc]FASTAAdd to Basket

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    MRFYAVGLNH ECTSLEQTET FALSAEEQEA LYANLSLSAD AEVVVLSTCN    50
    RTEAYLYGTE ADLRQVKALI GQGGGTRWPE ETAFQERDEA AVRHLLQVTS 100
    GLRSVVLGER QIFAQVKAAY ERAVDAGGIH SVMHRLFHTA FRAAKRVSSE 150
    TGLGRGAASV STAAVEMARQ DLSEAGGEGL RNTEIVLVGA GKMGRLALEA 200
    LADESLASLT VVNRSPDRAR EVASPFGGDT EPWADRHRAV ATADLALVAT 250
    GASDPVLHAP ALPAPDEATL VVDVAMPRNV DPAVDERPGY RLYDLDDLEA 300
    WTAEVRERRA DAVPEAESIC EELLEDFVTW VFHQQALQPA IQAIRSTFDT 350
    IREQEVDRHA HRTGMDREEV DRLTESIMQK LLAVPIVRLK NVDPESIDFV 400
    QGIELLHALF APSDESDAGR SLAEAPDADT PDLGEAPSRC PYMTHDPGGD 450
    GTETEEVQKA LRLSAAHQAA SHSEEVRGG 479
    Length:479
    Mass (Da):51,933
    Last modified:May 20, 2008 - v2
    Checksum:iCCBDCF4F287BBB5D
    GO

    Sequence cautioni

    The sequence ABC43868.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000159 Genomic DNA. Translation: ABC43868.1. Different initiation.
    RefSeqiYP_445676.1. NC_007677.1.

    Genome annotation databases

    EnsemblBacteriaiABC43868; ABC43868; SRU_1555.
    GeneIDi3851349.
    KEGGisru:SRU_1555.
    PATRICi23425545. VBISalRub86502_1609.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000159 Genomic DNA. Translation: ABC43868.1 . Different initiation.
    RefSeqi YP_445676.1. NC_007677.1.

    3D structure databases

    ProteinModelPortali Q2S2A5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 309807.SRU_1555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC43868 ; ABC43868 ; SRU_1555 .
    GeneIDi 3851349.
    KEGGi sru:SRU_1555.
    PATRICi 23425545. VBISalRub86502_1609.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000106238.
    KOi K02492.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci SRUB309807:GJJD-1552-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: DSM 13855 / M31.

    Entry informationi

    Entry nameiHEM1_SALRD
    AccessioniPrimary (citable) accession number: Q2S2A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 74 of the entry and version 2 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