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A0AJ06

- HEM1_LISW6

UniProt

A0AJ06 - HEM1_LISW6

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (28 Nov 2006)
      Previous versions | rss
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    • Comment

    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

    BioCyciLWEL386043:GI5X-1592-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:lwe1570
    OrganismiListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
    Taxonomic identifieri386043 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000000779: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 437437Glutamyl-tRNA reductasePRO_1000004632Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi386043.lwe1570.

    Structurei

    3D structure databases

    ProteinModelPortaliA0AJ06.
    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.
    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.

    A0AJ06-1 [UniParc]FASTAAdd to Basket

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    MFILTMGLNH HTAPIDIREK LVFKETEEEM ALITLLQEKS ILENVIISTC    50
    NRTEIVAVVD QIHTGRYYLK RFMANWFQMD MEKIEPYLFF HEEKEAVNHL 100
    YKVTAGLDSL VLGETQILGQ VKHAFEIAKQ TGTTGTLLNK LFREVVTFAK 150
    KVHHQTKINE NAVSVSYAAV EVAKKLYGSL ENKKIVLVGA GEMSELALQN 200
    LAGSGIADIT IINRTKANAE ILADQFQAKV GTYEEMNNYL SIADIVLVST 250
    SADEPIIKQK DMQILMSQKS TSMLVIDIGL PRNVEHDCSY IPNFHLYDID 300
    DLAGVVSANS LERQKIVLAL ENTIETEVQN FFEWEKQLGV VPVIRALREK 350
    ALEMQEITMT SLENKLPGLT EREYIQIGKH MKSIINQMLK QPISELKEMS 400
    VENDAPTSIE HFKRIFGLTE LDITLSEKTQ EQAETRS 437
    Length:437
    Mass (Da):49,491
    Last modified:November 28, 2006 - v1
    Checksum:iE16282612A8B251C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM263198 Genomic DNA. Translation: CAK20988.1.
    RefSeqiYP_849767.1. NC_008555.1.

    Genome annotation databases

    EnsemblBacteriaiCAK20988; CAK20988; lwe1570.
    GeneIDi4465230.
    KEGGilwe:lwe1570.
    PATRICi20330283. VBILisWel39304_1576.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM263198 Genomic DNA. Translation: CAK20988.1 .
    RefSeqi YP_849767.1. NC_008555.1.

    3D structure databases

    ProteinModelPortali A0AJ06.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 386043.lwe1570.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAK20988 ; CAK20988 ; lwe1570 .
    GeneIDi 4465230.
    KEGGi lwe:lwe1570.
    PATRICi 20330283. VBILisWel39304_1576.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci LWEL386043:GI5X-1592-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. "Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
      Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.
      , Lampidis R., Kreft J., Goebel W., Chakraborty T.
      J. Bacteriol. 188:7405-7415(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35897 / DSM 20650 / SLCC5334.

    Entry informationi

    Entry nameiHEM1_LISW6
    AccessioniPrimary (citable) accession number: A0AJ06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 65 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