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B5FBW9

- HEM1_VIBFM

UniProt

B5FBW9 - HEM1_VIBFM

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Vibrio fischeri (strain MJ11)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (14 Oct 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 sitei50 – 501NucleophileUniRule 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

    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:VFMJ11_0803
    OrganismiVibrio fischeri (strain MJ11)
    Taxonomic identifieri388396 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
    ProteomesiUP000001857: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418Glutamyl-tRNA reductasePRO_1000093177Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi388396.VFMJ11_0803.

    Structurei

    3D structure databases

    ProteinModelPortaliB5FBW9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate 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.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    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. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B5FBW9-1 [UniParc]FASTAAdd to Basket

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    MSLLVIGINH TSASVDLREK VAFSPEKLTK ALDELKNSDA IQSGVILSTC    50
    NRTEIYCEVK HGISSGYVIN WLAEFHHVAL EILMPSIYIH EEQAAVKHLM 100
    RVSCGLDSLV LGEPQILGQV KKAFADAREH NAVEGTIEKL FQQDFSVAKR 150
    VRTETNIGGN AVSVAYAACT LARQIFESLS DSTVLLVGAG ETIELVAKHL 200
    DDSGCKRLIV ANRTRERAMG LAEQFNAEVI SLPEIPEHLP KADIIISSTA 250
    SPLPIIGKGM VESALKLRKH QPMLFVDIAV PRDIEGEVAE LNDAYLYSVD 300
    DLQSIIDHNI EQRKIEAIQA EAIVSEESAE FMTWIRSRQA VNSIRQYREN 350
    SEAMRIELLQ KSMQALASGQ NPEKVLAELS NKLTNKLIHA PTLAMQQAAK 400
    NGETEKLTVI RTTIGLDN 418
    Length:418
    Mass (Da):46,067
    Last modified:October 14, 2008 - v1
    Checksum:iB43CB77DF3375636
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001139 Genomic DNA. Translation: ACH65238.1.
    RefSeqiYP_002155528.1. NC_011184.1.

    Genome annotation databases

    EnsemblBacteriaiACH65238; ACH65238; VFMJ11_0803.
    GeneIDi6805479.
    KEGGivfm:VFMJ11_0803.
    PATRICi20120069. VBIVibFis37164_0756.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001139 Genomic DNA. Translation: ACH65238.1 .
    RefSeqi YP_002155528.1. NC_011184.1.

    3D structure databases

    ProteinModelPortali B5FBW9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 388396.VFMJ11_0803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACH65238 ; ACH65238 ; VFMJ11_0803 .
    GeneIDi 6805479.
    KEGGi vfm:VFMJ11_0803.
    PATRICi 20120069. VBIVibFis37164_0756.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    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. "Complete sequence of Vibrio fischeri strain MJ11."
      Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MJ11.

    Entry informationi

    Entry nameiHEM1_VIBFM
    AccessioniPrimary (citable) accession number: B5FBW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 49 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3