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Q252N9

- HEM1_CHLFF

UniProt

Q252N9 - HEM1_CHLFF

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydophila felis (strain Fe/C-56)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (18 Apr 2006)
      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 sitei51 – 511NucleophileUniRule annotation
    Sitei92 – 921Important for activityUniRule annotation
    Binding sitei102 – 1021SubstrateUniRule annotation
    Binding sitei113 – 1131SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi181 – 1866NADPUniRule 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

    BioCyciCFEL264202:GJCG-1016-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:CF0977
    OrganismiChlamydophila felis (strain Fe/C-56)
    Taxonomic identifieri264202 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
    ProteomesiUP000001260: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 338338Glutamyl-tRNA reductasePRO_0000335021Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi264202.CF0977.

    Structurei

    3D structure databases

    ProteinModelPortaliQ252N9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate bindingUniRule annotation
    Regioni107 – 1093Substrate 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.
    HOGENOMiHOG000110628.
    KOiK02492.
    OMAiCHRAELY.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    [Graphical view]
    PfamiPF05201. GlutR_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF69742. SSF69742. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q252N9-1 [UniParc]FASTAAdd to Basket

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    MVLGVVGISY REAALKEREA VINILKTFEA DTLLAQRFFG GDGSFVLLLT    50
    CHRAEIYYFS KSNANVQSKL LSWISSLGTR PYCYQGLACF THLFTVTSGM 100
    DSLIFGETEI QGQVKRAYIK AKTDRELPFA LHFLFQKALK EGKDFRSQVS 150
    LSYPVVTMES IVEETLDLHG KSTKDKLLFI GYSDVNRKIA KGLSAKGYRN 200
    LIFCSRKNIP IPYDTVARSQ LSFGKPYDVI FFGSSESARD FPGLSLESLA 250
    GIPNRVVFDF NVPRTFTLVE RPEGISYLDM DFISERVQKK LQISKQCTNK 300
    EKPFLALAAR KQWEVYEKKS SNISLSQIRT SRPKLLIL 338
    Length:338
    Mass (Da):38,262
    Last modified:April 18, 2006 - v1
    Checksum:i514B1BAA1E41A3B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006861 Genomic DNA. Translation: BAE81749.1.
    RefSeqiWP_011458522.1. NC_007899.1.
    YP_515894.1. NC_007899.1.

    Genome annotation databases

    GeneIDi3958483.
    KEGGicfe:CF0977.
    PATRICi20205669. VBIChlFel51660_1026.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006861 Genomic DNA. Translation: BAE81749.1 .
    RefSeqi WP_011458522.1. NC_007899.1.
    YP_515894.1. NC_007899.1.

    3D structure databases

    ProteinModelPortali Q252N9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264202.CF0977.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3958483.
    KEGGi cfe:CF0977.
    PATRICi 20205669. VBIChlFel51660_1026.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000110628.
    KOi K02492.
    OMAi CHRAELY.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CFEL264202:GJCG-1016-MONOMER.

    Family and domain databases

    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    [Graphical view ]
    Pfami PF05201. GlutR_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69742. SSF69742. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fe/C-56.

    Entry informationi

    Entry nameiHEM1_CHLFF
    AccessioniPrimary (citable) accession number: Q252N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: April 18, 2006
    Last modified: October 1, 2014
    This is version 60 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