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A8ERT8

- HEM1_ARCB4

UniProt

A8ERT8 - HEM1_ARCB4

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Arcobacter butzleri (strain RM4018)
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 (13 Nov 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 sitei51 – 511NucleophileUniRule annotation
    Sitei100 – 1001Important for activityUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation
    Binding sitei121 – 1211SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1956NADPUniRule 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

    BioCyciABUT367737:GHWO-386-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:Abu_0387
    OrganismiArcobacter butzleri (strain RM4018)
    Taxonomic identifieri367737 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter
    ProteomesiUP000001136: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Glutamyl-tRNA reductasePRO_1000057569Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi367737.Abu_0387.

    Structurei

    3D structure databases

    ProteinModelPortaliA8ERT8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate bindingUniRule annotation
    Regioni115 – 1173Substrate 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.
    OMAiHEVTGEY.
    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.

    A8ERT8-1 [UniParc]FASTAAdd to Basket

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    MSYLVISFSH KNTDIKLREK LAFNSDEDKD RFLKLILEND ITKEAILLST    50
    CNRVEIITRS LNIKQSSKDI IEKLATYSKV DFDVLYDRAD IYDADGAVHH 100
    LFSVASALDS LVIGETQIVG QLKDAFRFSQ AKGYCSLNIT RVMHYAFKCA 150
    AQVRTATSLG TGSVSVASTA VSKAKDIIGN TKDVKALVVG AGEMSELTVK 200
    HLIASGFDVT IISRDTKKAQ NLASTFEVHV NVEPYDKLTQ LLITTPIMIT 250
    ATSAPYPIIT KENAPSSNIN RYWFDIAVPR DIDENISMSN LEIFSVDDLQ 300
    DIVNENMSLR AEQAKTAYGI VSRMSLEFFE WLKSLEIEPI VKNLYLKGNE 350
    IIDKKVKNAI KKGFIDSKDE ENIRKLCLTV ITEYLHNPAK QLKDISKNME 400
    CDLVVGTVQN MFSLNENSTS KNRYKCDHLS KN 432
    Length:432
    Mass (Da):48,438
    Last modified:November 13, 2007 - v1
    Checksum:iE7753AA710ECAB7B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000361 Genomic DNA. Translation: ABV66662.1.
    RefSeqiWP_012012216.1. NC_009850.1.
    YP_001489331.1. NC_009850.1.

    Genome annotation databases

    EnsemblBacteriaiABV66662; ABV66662; Abu_0387.
    GeneIDi5624856.
    KEGGiabu:Abu_0387.
    PATRICi20962134. VBIArcBut20197_0380.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000361 Genomic DNA. Translation: ABV66662.1 .
    RefSeqi WP_012012216.1. NC_009850.1.
    YP_001489331.1. NC_009850.1.

    3D structure databases

    ProteinModelPortali A8ERT8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 367737.Abu_0387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV66662 ; ABV66662 ; Abu_0387 .
    GeneIDi 5624856.
    KEGGi abu:Abu_0387.
    PATRICi 20962134. VBIArcBut20197_0380.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi HEVTGEY.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci ABUT367737:GHWO-386-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. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RM4018.

    Entry informationi

    Entry nameiHEM1_ARCB4
    AccessioniPrimary (citable) accession number: A8ERT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: November 13, 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