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Q92BF7

- HEM1_LISIN

UniProt

Q92BF7 - HEM1_LISIN

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Listeria innocua serovar 6a (strain CLIP 11262)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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
    Sitei99 – 991Important for activityUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule 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

    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:lin1592
    OrganismiListeria innocua serovar 6a (strain CLIP 11262)
    Taxonomic identifieri272626 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000002513: Chromosome

    Organism-specific databases

    GenoListiLIN1592.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Glutamyl-tRNA reductasePRO_0000114035Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272626.lin1592.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92BF7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni114 – 1163Substrate 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.
    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.

    Q92BF7-1 [UniParc]FASTAAdd to Basket

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    MFILTMGLNH HTAPIDIREK LVFKETEEEM ALVTLLQEKS ILENVIISTC    50
    NRTEIVAVVD QIHTGRYYLK RFMANWFQMD MEKIEPYLFF HEEAEAVNHL 100
    YKVTAGLDSL VLGETQILGQ VKHAFEIAKQ TGTTGTLLNK LFREVVTFAK 150
    KVHHHTKINE NAVSVSYAAV EVAKKLYGSL DNKKIVLIGA GEMSELALQN 200
    LAGSGIADIT IINRTKSNAE ILAHQFQAKV GAYENMSDHL LEADIVLVST 250
    SAEEPIIKQV AMQELMEQKA SSMLVIDIGL PRNVEHDCSY IPNFHLYDID 300
    DLAGVVSANS LERQRIVQEL ENTIETEVRS FFEWEKQLGV VPVIRALREK 350
    ALDMQEVTMT SLENKLPGLT EREYIQIGKH MKSIINQMLK QPISELKEMS 400
    VEENADTSIE HFKRIFGLTE TDVAIIEKEQ AETRS 435
    Length:435
    Mass (Da):49,228
    Last modified:December 1, 2001 - v1
    Checksum:iED4697E1E2C954E4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL596169 Genomic DNA. Translation: CAC96823.1.
    PIRiAG1631.
    RefSeqiNP_470928.1. NC_003212.1.

    Genome annotation databases

    EnsemblBacteriaiCAC96823; CAC96823; CAC96823.
    GeneIDi1130212.
    KEGGilin:lin1592.
    PATRICi20299921. VBILisInn102668_1627.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL596169 Genomic DNA. Translation: CAC96823.1 .
    PIRi AG1631.
    RefSeqi NP_470928.1. NC_003212.1.

    3D structure databases

    ProteinModelPortali Q92BF7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272626.lin1592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC96823 ; CAC96823 ; CAC96823 .
    GeneIDi 1130212.
    KEGGi lin:lin1592.
    PATRICi 20299921. VBILisInn102668_1627.

    Organism-specific databases

    GenoListi LIN1592.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CLIP 11262.

    Entry informationi

    Entry nameiHEM1_LISIN
    AccessioniPrimary (citable) accession number: Q92BF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 96 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