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Q63QF1

- HEM1_BURPS

UniProt

Q63QF1 - HEM1_BURPS

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Burkholderia pseudomallei (strain K96243)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      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 sitei65 – 651NucleophileUniRule annotation
    Sitei113 – 1131Important for activityUniRule annotation
    Binding sitei123 – 1231SubstrateUniRule annotation
    Binding sitei134 – 1341SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi203 – 2086NADPUniRule 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

    BioCyciBPSE272560:GJNI-3156-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:BPSL3072
    OrganismiBurkholderia pseudomallei (strain K96243)
    Taxonomic identifieri272560 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000000605: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Glutamyl-tRNA reductasePRO_0000114001Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272560.BPSL3072.

    Structurei

    3D structure databases

    ProteinModelPortaliQ63QF1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 674Substrate bindingUniRule annotation
    Regioni128 – 1303Substrate 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.
    OMAiKMLHGTM.
    OrthoDBiEOG6C2WN5.

    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.

    Q63QF1-1 [UniParc]FASTAAdd to Basket

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    MGLNDSLLDM QLLTIGINHH TAPVALRERV AFPLEQIKPA LSTFKSVFLG    50
    HPAPNAPEAA ILSTCNRTEL YCATNDRAAR DAAIRWMSDY HRIPADELAP 100
    HVYALPQSEA VRHAFRVASG LDSMVLGETQ ILGQMKNAVR TASEAGSLGT 150
    YLNQLFQRTF AVAKEVRGTT EIGAQSVSMA AAAVRLAQRI FEQVAQQRVL 200
    FIGAGEMIEL CATHFAAQGP RELVVANRTA ERGAKLAERF GGRAMPLADL 250
    PARMHEFDII VSCTASTLPI IGLGAVERAV KARRHRPIFM VDLAVPRDIE 300
    PEVGKLKDVF LYTVDDLGAI VREGNASRQA AVAQAEAIIE TRVQNFMQWL 350
    DARSIVPVIR HMHTQADALR RAEVERARKM LARGDDPDAV LDALSQALTN 400
    KLIHGPTSAL NRANGADRDS LIDLMRGFYQ HAPRSSDTSD R 441
    Length:441
    Mass (Da):48,258
    Last modified:October 25, 2004 - v1
    Checksum:i06D2A7C3C3F1D032
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571965 Genomic DNA. Translation: CAH37083.1.
    RefSeqiYP_109667.2. NC_006350.1.

    Genome annotation databases

    EnsemblBacteriaiCAH37083; CAH37083; BPSL3072.
    GeneIDi3094369.
    KEGGibps:BPSL3072.
    PATRICi19266651. VBIBurPse99623_3515.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX571965 Genomic DNA. Translation: CAH37083.1 .
    RefSeqi YP_109667.2. NC_006350.1.

    3D structure databases

    ProteinModelPortali Q63QF1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272560.BPSL3072.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH37083 ; CAH37083 ; BPSL3072 .
    GeneIDi 3094369.
    KEGGi bps:BPSL3072.
    PATRICi 19266651. VBIBurPse99623_3515.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi KMLHGTM.
    OrthoDBi EOG6C2WN5.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci BPSE272560:GJNI-3156-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: K96243.

    Entry informationi

    Entry nameiHEM1_BURPS
    AccessioniPrimary (citable) accession number: Q63QF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 77 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