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C5C5B0

- HEM1_BEUC1

UniProt

C5C5B0 - HEM1_BEUC1

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      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
    Sitei114 – 1141Important for activityUniRule annotation
    Binding sitei124 – 1241SubstrateUniRule annotation
    Binding sitei135 – 1351SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi204 – 2096NADPUniRule 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

    BioCyciBCAV471853:GI1Z-4062-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:Bcav_4009
    OrganismiBeutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
    Taxonomic identifieri471853 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeBeutenbergiaceaeBeutenbergia
    ProteomesiUP000007962: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Glutamyl-tRNA reductasePRO_1000202630Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi471853.Bcav_4009.

    Structurei

    3D structure databases

    ProteinModelPortaliC5C5B0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 514Substrate bindingUniRule annotation
    Regioni129 – 1313Substrate 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.
    HOGENOMiHOG000109649.
    KOiK02492.
    OMAiPYLYVHY.
    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.
    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. 2 hits.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C5C5B0-1 [UniParc]FASTAAdd to Basket

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    MLLSVSASHR DADLADLERL SSGVGRVWAD APLVAHGLDG AGVVLLATCN    50
    RFEVYLDVAD GTDPQRALAV VRDLVRTVPE SPLAAPGADD DAAGPGPDPS 100
    AALRVRVGDD AARHLFGVAS GLDSIVVGER EIAGQVRRAI AAARRAGTTT 150
    GALERLFAQA QRTSRAVEAG TGLAAAGRSV VGVALDLAAR SAPPWPLARV 200
    VLIGTGSYAG ASLAALRARG CTDVRVHSES GRAEEFARAR EAEAVPPGEL 250
    LTAIADADVV VSCRGSVRPV LDAAAVAGAR AAAERRAEER AGHAVGTAVQ 300
    PRPLVVVDLA LHRDVDPAVG SVDGVELLDL GTIRAHAPAA ATRDVERARE 350
    IVDDAVAQHA LVRAAREMDP AITRLRGRVR EVLDAEVGRL PVGPVSREDA 400
    ERALHRLAAT LAHAPTEAAR EAARAGRGEE YVEALRLLFP D 441
    Length:441
    Mass (Da):45,703
    Last modified:July 28, 2009 - v1
    Checksum:i0AF8243E92066449
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001618 Genomic DNA. Translation: ACQ82250.1.
    RefSeqiYP_002884012.1. NC_012669.1.

    Genome annotation databases

    EnsemblBacteriaiACQ82250; ACQ82250; Bcav_4009.
    GeneIDi7861107.
    KEGGibcv:Bcav_4009.
    PATRICi21098740. VBIBeuCav91323_4061.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001618 Genomic DNA. Translation: ACQ82250.1 .
    RefSeqi YP_002884012.1. NC_012669.1.

    3D structure databases

    ProteinModelPortali C5C5B0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 471853.Bcav_4009.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACQ82250 ; ACQ82250 ; Bcav_4009 .
    GeneIDi 7861107.
    KEGGi bcv:Bcav_4009.
    PATRICi 21098740. VBIBeuCav91323_4061.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109649.
    KOi K02492.
    OMAi PYLYVHY.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci BCAV471853:GI1Z-4062-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. 2 hits.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-8 / DSM 12333 / NBRC 16432.

    Entry informationi

    Entry nameiHEM1_BEUC1
    AccessioniPrimary (citable) accession number: C5C5B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 43 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